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Preface for Volume 2
Volume 2 contains chapters on the biological and medical aspects of vitamin B12,
including transport in microorganisms and man and the quantitation of cobalamins
in human serum. In addition, each of the major coenzyme B12-dependent enzymatic reactions are discussed, including methyl transfer, acetate and methionine
biosynthesis, amino mutases, diol dehydrase, ethanolamine ammonia-lyase, ribonucleolide reductase, and the glutamate and methylmalonyl-CoA mutases. Metalfree corrinoids and metal insertion are also covered.
The final result is an up-to-date and critical review of the areas described above.
This treatise provides, for the first time, a complete and comprehensive review of all
of the major chemical, biochemical, and medical aspects of vitamin B12.
I wish to take this opportunity to thank the contributors to this volume for
both the scholarship of their work and the promptness with which they all met the
various deadlines.
DAVID DOLPHIN
Vancouver, British Columbia
November 1981
General Preface
The vitami n B coenzyme and related corrinoid s represent the most complex nonpolymeric structures foun d i n nature , and in addition they are th e onl y known naturally occurring organometalli c complexes . Their uniquenes s an d complexity have
presented majo r challenges, and will continue so to do for some time to come, in all
areas o f the natural and life sciences . Indeed, solutions to B 1 2-related problems present some of the principal scientific achievements of the past half century ; each
decade has recorded a milestone toward s an understanding of the nature and func tion o f these systems .
In 1926 Minot an d Murphy announced a dietary treatment of pernicious ane mia, which ha d previousl y proved t o b e a fatal disease. In 1934 they were awarded
the Nobel Prize for their discoveries concerning liver therapy against anemias . I n
1948 Folker' s grou p i n th e Unite d States an d Leste r Smith' s in Great Britain independently announced th e isolatio n and crystallization o f the re d antiperniciou s anemia facto r no w know n as vitamin B . The structure of vitamin B wa s revealed in
1956 b y th e X-ra y crystallographi c work o f Hodgkin's grou p an d b y the chemical
studies o f Todd an d Johnson . I n 1958 Barker isolated and characterized coenzyme
B 1 2 , showing that vitami n B (cyanocobalamin ) is an antifact generated during its
isolation. The structure of the coenzym e wit h its uniqu e cobalt-carbon bond wa s
elucidated once mor e b y Hodgki n i n 1961 . The 1960s saw majo r advance s in our
understanding o f both the chemistry and enzymology of B and it s coenzyme ,
culminating in th e total synthesis of vitamin B b y Woodward and Eschenmoser in
1976.
1 2
1 2
! 2
1 2
1 2
1 2
Since there are fewer molecule s o f B i n a ma n than there are red blood cells,
it i s not surprisin g tha t there is still much to learn about this molecule. This is especially true i n mammal s where the function of B i n such low concentrations is still
unclear. Furthermore , although there are many enzymatic reactions dependent on
coenzyme B , its mechanism of action is still obscure.
This wor k consists of two volumes and cover s al l o f th e major aspect s o f th e
chemistry, biochemistry, and medicine relating to B . Volume 1 emphasizes chemistry, biosynthesis , history , and nomenclature ; Volum e 2 cover s biochemical an d
medical aspects .
I wish t o than k Dr . Olg a Avramovic fo r her assistance, Alan Johnson for introducing me t o B , and th e late R. B. Woodward for expanding and encouraging my
knowledge an d interes t i n th e subject .
1 2
t 2
1 2
J 2
1 2
D A V I D DOLPHIN
Vancouver, British Columbia
November 1981
Contents
1
Biological and Medical Aspects of Vitamin B12
William S. Beck
1
Evolutionary Aspects, 1
2
Sources of Cobalamins in Nature, 3
3
Distribution of Cobalamins in Nature, 6
4
Cobalamin Patterns in Man, 12
References, 23
2
Cobalamin Transport in Microorganisms
Clive Bradbeer
1
Introduction, 32
2
Bacterial Transport of Cobalamin, 33
3
Eucaryotic Transport of Cobalamin, 50
References, 52
3
Instrinsic Factor, Transcobalamin, and Haptocorrin
Ebba Nexǿ and Henrik Olesen
1
Introduction, 57
2
Nomenclature, 58
3
Purification, 59
4
Structure, 63
5
Cobalamin-Binding Site, 68
6
Immunology, 70
7
Physiology, 70
8
Concluding Remarks, 76
References, 77
4
Quantitation of Cobalamins in Human Serum
Ebba Nexǿ and Henrik Olesen
1
Introduction, 88
2
Evaluation of Method, 88
3
Extraction of Cobalamins, 89
4
Calibration Standards, Tracer, and Control Material, 92
5
Microbiological Assays, 93
6
Isotope Dilution Assays, 94
7
Comparison of Results from Different Assays, 97
8
Reference Intervals, 98
9
Clinical Usefulness, 98
10
Quantitation of Cobalamins Bound to Haptocorrin and
Transcobalamin, 98
11
Quantitation of Different Forms of Cobalamin, 99
12
Concluding Remarks, 99
References, 100
5 Metal-Free Corrinoids and Metal Insertion 105
Volker B. Koppenhagen
1
Introduction, 106
2
Naturally Occurring Metal-Free Corrinoids, 106
3
Descobaltocorrinoid-c-Lactams and c-Lactones, 111
4
Synthetic Metal-Free Corrinoids, 112
5
Absorption Spectra, 113
6
Reactions with Alkali, 114
7
Metal Insertion, 120
8
Biological Properties, 139
9
Biotransformation, 142
10 Metal-Free Corrinoids and Vitamin B 12 Biosynthesis, 143
References, 146
6 Mechanisms for B 12 -Dependent Methyl Transfer 151
J. M. Wood
1
Introduction, 151
2
Electrophilic Attack on the Co—C Bond of Methylcobalamin, 154
3
Free Radical Attack on the Co—C Bond of Methylcobalamin, 155
4
Lablilization of the Co—C Bond by Outer Sphere Interactions
with the Corrin Ring, 156
5
6
Nucleophilic Attack on the Co—C Bond of Methylcobalamin, 160
Concluding Remarks, 160
References, 162
7
Acetate Biosynthesis 165
Lars G. Ljungdahl and Harland G. Wood
1
Introduction, 166
2
Acetogenic Bacteria, 167
3
The Corrinoid Pathway of Synthesis of Acetate, 172
4
A Note on Corrinoid Biosynthesis in C thermoaceticwn, 191
5
The Glycine Decarboxylase (Noncorrinoid) Pathway of
Synthesis of Acetate, 192
6
A Note on Electron Transport and Energy Metabolism in
Acetogenic Bacteria, 196
7
Concluding Remarks, 196
References, 197
8
Amino Mutases 203
John J. Baker and Thressa C. Stadtman
1
Introduction, 204
2
Mutases Catalyzing Migrations of co-amino Groups on
Diamino Acids, 206
3
L-Leucine-2,3-Aminomutase,
4
Concluding Comments, 229
227
References, 230
9
Diol Dehydrase 233
Tetsuo Toraya and Saburo Fukui
1
Introduction, 234
2
Properties of Diol Dehydrase, 235
3
Catalytic Properties of Diol Dehydrase, 238
4
Mechanism of Action of Diol Dehydrase, 242
5
Interaction of Diol Dehydrase with B 12 Coenzymes, 246
6
Physiological Significance of Diol Dehydrase and Its Relationship
with Glycerol Dehydrase, 253
7
Regulation of the Apoenzyme Synthesis and Enzyme Activity, 257
8
Concluding Remarks, 258
References, 259
10
Ethanolamine Ammonia-Lyase 263
Bernard M. Babior
1
History, 264
2
Preparation and Assay of the Enzyme, 265
3
Structure of the Enzymes, 266
4
Reactions Catalyzed by Ethanolamine Ammonia-Lyase, 266
5
The Mechanism of Action of Ethanolamine Ammonia-Lyase, 271
References, 286
11 Glutamate Mutase
298
Robert L. Switzer
1
Introduction, 289
2
Assays for Glutamate Mutase, 291
3
Purification of the Glutamate Mutase Components, 292
4
Physical and Chemical Properties of the Glutamate Mutase
Components, 292
5
Kinetic Properties of the Glutamate Mutase System, 293
6
7
Interaction and Function of the Glutamate Mutase
Components, 295
Studies of the Mechanism of the Glutamate Mutase Reaction, 297
8
Conclusions, 302
References, 303
12 B12-Dependent Methionine Biosynthesis 307
Robert T. Taylor
1
Introduction, 308
2
Escherichia coli B 12 Methyltransferase (Methionine Synthetase), 309
3
Properties of Other Microbial B 12 Methionine Synthetases, 339
4
Mammalian B12 Methyltransferases, 339
5
Conclusions, 347
References, 348
13 Methylmalonyl-CoA Mutase 357
János Retey
1
Introduction, 358
2
Biological Functions and Sources of Methylmalonyl-CoA
Mutase, 358
3
Isolation of Methylmalonyl-CoA Mutase, 360
4
5
Assay of Methylmalonyl-CoA Mutase, 368
Physical and Chemical Properties, 365
6
Mechanistic Studies, 367
7 Conclusions, 376
References, 376
14 Cobalamin-DependentRibonucleotideReductases 381
Raymond L. Blakley
1
Introduction, 382
2
Distribution of the Enzyme in Nature, 383
3
Biochemical Role of the Enzyme, 385
4
Purification, 386
5
Assay of the Reductase, 389
6
Physical and Chemical Properties of Cobalamin-Dependent
Reductases, 391
7
Mechanism of Action, 402
8
Conclusion, 414
References, 414
CONTENTS OF VOLUME 1
1
History of Vitamin B12: Pernicious Anemia to Crystalline Cyanocobalamin
Karl Folkers
2
Nomenclature
Waldo E. Cohn
3
X-Ray Crystallography of B12 and Cobaloximes
Jenny Pickworth Glusker
4
Biosynthesis of the Corrin Macrocycle
Alan R. Battersby and Edward McDonald
5
Biosynthesis of Cobalamin Coenzymes
F. M. Huennekens t K. S. Vitols 1 K. Fujii and D. W. Jacobsen
6
The Total Synthesis of Vitamin B12
Robert V. Stevens
7
Reactions of the Corrin Macrocycle
Raymond Bonnett
8
Synthesis of Organocobalt Complexes
Kenneth L. Brown
9
Reactions of Alkyl Ligands Coordinated to Cobalamins and Cobaloximes
H. P. C. Hogenkamp
10
Coordination Chemistry of the B12 Dependent Isomerase Reactions
J. M. Pratt
11
Electronic Spectra of B12 and Related Systems
C. Giannotti
12
EPR of B12 -Dependent Enzyme Reactions and Related Systems
John R. Pilbrow
13
The Nuclear Magnetic Resonance Spectroscopy of Cobalamins and
Their Derivatives
Otto D. Hensens f H. Allen 0. Hill t Charlotte E. McClelland
and Robert J. P. Williams
14
Chemistry and Significance of Vitamin B12 Model Systems
Jack Halpern
15
Mechanisms of Action of the B12 Coenzyme: Theory and Models
Bernard T. Golding
Author Index
Numbers inparentheses are reference numbers and indicate that the author's work is referred to
although his name may not be mentioned in the text. Numbers in italics indicate pages
on which complete references are listed.
Aaronson, S., 11(120), 27, 50(82, 84),
51(86), 55
Abbott, L.D., 22(214), 30
Abe, T., 74(149), 82
Abeles, R. H., 7(53), 21(210), 30, 59(26),
78, 234(4, 5), 235(5, 6, 9, 10), 236
(12), 239(18, 23), 240(5, 26, 27),
241(5), 242(5, 32, 33, 34, 37), 243(12,
18, 23, 38, 40, 41, 42, 43, 44), 244(9,
12, 26, 27, 41, 45, 46), 245(9, 34, 47,
48, 51), 246(5), 247(9, 60), 248(6, 9,
60), 249(73), 251(75), 256(4), 259, 260,
261, 262, 269(23), 271(30, 31), 272(23,
33, 34, 37), 273(37), 274(38), 275(42),
278(33,46), 280(53), 281(53), 283(33),
286,287,298(32,33), 299(32,33,35), 301
(35, 43, 44), 302(35), 304, 305, 310
(32), 311(32), 320(32), 339(119), 341
(129), 349, 352, 353, 359(6), 370(39, 40,
41, 43), 372(54), 376, 378, 383(16), 384
(16), 391(16), 402(16), 404(16, 102),
405(16), 409(112), 415, 418
Abels, J., 62(213), 71(61, 86), 79, 80, 84
Abley,P., 158(37), 163
Abraham, A., 50(76), 55
Abrams, R., 383(12), 384(12), 386(12,
54, 60), 387(60), 389(60, 74), 392
(60), 393(54), 394(60, 84), 395(60),
396(60), 397(60, 84), 405(60), 406
(101), 410(84), 415, 416, 417, 418
Adams, A., 383(14), 384(14), 389(14),
415
Adams, J. F., 13(138, 145), 20(204, 205,
215), 27, 30, 88(20), 96(58), 97(58),
101
Agnes, G., 155(16), 156(16), 157(25),
159(25), 163
Ahluwalia, B. K., 15(155), 28
Alexander, F., 12(127), 27
Alexander, W. F., 16(168), 28
Alizade, M. A., 373(62), 378
Allen, E. S., 91(42), 102
Allen, N. C, 7(61), 12(61), 17(61), 18
(176), 25, 29, 71(87), 80, 88(25), 95(25),
96(118), 97(25), 101, 104
Allen, R. H., 7(61), 12(61), 14(147, 151),
15(147, 153,160), 17(61,175), 18
(175,176, 177), 20(195),25, 28, 29,
58(2,6,9, 10), 61(2, 31,34,37),
63(37), 64(34, 37, 39,44, 215, 216,
218, 219, 220), 66(44), 67(6, 34),
68(49), 70(53), 71(6, 49, 63, 81, 87,
89), 72(89), 74(39, 142, 148, 153, 155),
75(164), 76(6, 189), 77, 78, 79, 80, 82,
83, 84, 85, 88(10,13, 25), 93(57),
95(25, 57), 96(112,118,119,121, 122),
97(25), 98(10), 100, 101,102, 104,
230(55), 232, 339(114), 340(122),
352, 363(22), 377
Allen, S . H.
G., 297(25), 304, 359(9),
361(13), 362 (17, 20), 363(13), 364
(20), 365(13), 366(13), 367(13), 377
Alles,G. A., 6(41), 24
Almon,L., 11(114), 2d
Alpers,D.H., 18(176), 29, 71(81, 87,
89, 91), 72(89, 91), 80, 96(118, 119),
104
Altschuler,T.,5(23),2J
Alworth, W. L., 5(16), 7(66, 68), 23, 25
Ames, G. F.-L., 47(54), 54
Amess, J. A. L., 345(183), 355
Amris, A., 75(162), 83
Andeman,S.,71(71), 79
Andersen, J., 74(140), 75(140), 76
(140), 82, 88(8), 89(8), 90(8), 99
(8), 100
Andersen, K.- J., 71(80), 72(120), 74(120),
80, 81
Andersen, M. P., 75(162), 83
Anderson, B. B., 88(3), 92(3), 98(89), 100,
103
Anderson, E. H., 42(43), 53
Anderson, W., 257(97), 262
Andreesen, J. R., 167(9), 168(9), 169(9,
27), 170(9, 34, 35), 172(55), 173(27, 61),
174(61, 64, 68, 69), 175(27), 195(27),
196(34),
198, 199, 200
Anh,N. R., 376(73)
,
379
Anton, D. L., 37(24), 53, 247(62a),
261
Arends, A., 71(61), 79
Arigoni, D., 222(36, 37), 231, 242(36),
243(39), 260, 268(22), 269(28), 278
(49), 283(28), 286, 287, 370(42), 372
(33, 51, 56, 57, 59), 373(63), 378
Arkun,S.N., 15(161), 28
Armitage,J.B., 37(20), 53
Arnstein, H. R. V., 50(80), 55
Arsenyan, F. G., 161(52), 164
Asbjarnsen, G., 93(52), 102
Ashe, H., 310(
30), 343 (147), 3 47(147),
349, 353
Ashwell, G., 18(178), 29,65(40), 76(190),
78, 84
Attrup Rasmussen, P., 72(115), 81
Aussein, H. A. A., 161(53), 164
Austad,W.l., 98(78), 103
Ayers , W. A., 8(78), 25
Babior, B. M., 3(8), 23, 68(48), 79, 93(125),
104, 223(40, 41), 231, 242(35), 244
(45), 260,265(2), 266(12, 15, 16, 17,
18), 267(5,12,19), 268(21, 22), 269
(19, 23, 24, 26, 27), 270(24, 27), 271
(29), 272(19, 21, 23, 27, 32, 33, 35,
36, 37), 273(37), 274(26, 38, 39, 40, 41),
275(24,26),276(26), 278(19,33, 47, 48),
279(50), 280(52), 281(19, 21, 24, 27,
29), 282(19, 20, 24, 26),283(15, 17,
33, 52, 56, 57), 284(15,48, 57), 286,
287
Bachovchin, W. W., 238(17), 239(17,
20), 240(17, 25), 243(17, 20), 244(25),
259, 260
Bailey, G., 97(75), 103
Baker , H., 11(120), 27, 50(82), 51(84), 55,
88(24), 97(24), 101
Baker j H. N., 7(66), 25
Baker, J. J., 207(17), 208(19, 20), 209
(19, 20), 210(19, 20), 211(19, 20),
212(19, 28), 213(19), 214(19), 215(19,
20), 216(20), 217(19, 20), 218(19, 30),
219(19), 220(19, 20), 223(19), 225(19,
20), 226(20), 227(20), 231
Balch, W. E., 166(6), 167(6), 168(6),
196(6), 198
Baldesten, A., 389(69), 47 7
Baligia 5 B. R., 6(37), 24
Balinska, M., 343(146), 353
Ball, E. W., 98(85), 103
Baltimore, B. G., 294(20), 296(20), 299
(20), 300(20, 37), 304, 305
Banks, R. G. S., 346(184), 355
Bar, R. S., 74(158), 83
Barenholdt, O., 72(116), 81
Baresi, L., 166(5), 198
Baril, L., 70(52, 54), 73(52), 75(52),
79
Barker, H. A., 5(22), 23,167(8, 10, 14),
168(10, 23, 24), 169(26, 28), 170(10, 23,
24, 37, 38, 41, 42, 43), 171(43, 45, 46,
47), 192(10), 194(10), 198, 205(8, 9),
206(12), 207(15, 16, 17), 213(15), 223
(38), 230(50, 51, 52, 53), 231, 232,
290(3, 4, 5, 6, 7, 8), 291(4, 10,11, 12,
13,14, 15),292(11, 12,13, 16),293
(10, 11, 12, 13, 14),294(13, 14, 17,18,
20), 295(10, 11, 13, 14), 296(12, 13,20),
297(26, 27), 298(12, 16, 30, 31), 299
(20, 36), 300(13, 20, 37), 303, 304, 305,
309(24), 314(44), 349, 350, 358(3), 376,
383(10), 384(10), 415
Barkhan, P., 88(6), 90(6), 91(6), 92(6),
97(6, 76), 98(90), 100,103
Barness, L. E., 359(6), 376
Barnett, B. H., 11(119), 27, 386(57),
416
Barrels, H., 71(84), S0
Bash, R., 89(32), 96(32), 101
Baskerville, A. B., 75(170), 83
Bassford, P. J., 35(14), 36(14), 40(31, 34)
41(35), 42(31), 43(35,46), 44(14), 52,
53
Batterham, T. J., 402(100), 404(100),
418
Battersby, A. R., 5(18), 23,144(53),
149
Bayer, M. E., 40(32), 53
Becher,E.,5(20, 24), 25, 24
Beck, J. V., 167(10), 168(10, 23), 170
(10, 23), 192(10), 194(10), 198
Beck, R. A., 6(34, 38), 24
Beck, W. S., 2(4), 7(54, 58), 9(95), 11(118,
119), 17(171, 172, 174), 18(95, 179, 180),
20(95), 23, 24, 25, 26, 27, 28, 29, 49(60,
63), 54,157(24), 163, 383(16), 384(13,
16), 385(48, 50), 386(13, 48, 57, 58, 59),
387(59), 389(13, 48), 391(16, 50), 392
(59), 393(50, 59), 394(50), 395(50), 399
(13, 50), 402(16, 99), 404(16, 99, 102),
405(16), 415, 416, 418
Becker, CM., 18(179), 29
Becker, W., 123(30), 148
Beckham, T. M., 410(117), 411(117), 418
Begley, J. A., 70(56, 57), 72(119), 74(161),
75(56, 172), 76(198), 79, 81, 83, 84, 88
(19), 98(96), 99(99), 101,103, 104
Behrens, U., 51(86), 55
Beinert, H., 269
(26), 27 4(26), 2 75(26),
276(26), 282(26 ), 286, 301(42), 305,
407(108, 109), 408(108), 418
Beisbarth 5 H., 37(21), 53
Bell, M. C, 12(136), 13(136), 27, 71(66),
79
Bellama, J.M., 161(46), 164
Belt, M., 7(51), 24
Bender-Gotze, Ch., 71(84), 80
Bendle, S., 157(23), 159(23), 163
Benson, R. E., 15(156), 28
Benziman, M., 192(128), 202
Berger,E. A., 45(49), 54
Berglund, O., 388(67), 417
Bernhauer, K., 5(20, 24), 6(36), 7(52), 23,
24, 37(21), 53,130(36), 139(36), 145
(36), 148, 279(51), 287, 309(22), 349
Bernstein, L. H., 94(54), 102
Bertino, J. R., 342(135), 345(182), 347
(182,191), 353, 355
Bevan,G.,71(71), 79
Bhagaran, H. N., 6(37), 24
Bhan, A., 386(60), 387(60), 389(60), 392
(60), 394(60), 395(60), 396(60), 397(60),
405(60), 416
Bianchini, P., 99(104), 104
Biavati,B., 170(36), 199
Bidlingmaier, G., 374(64), 379
Bieganowski, R., 138(40, 41), 139(41), 148
Bieri, J. G., 339(111), 340(111), 341(111),
352
Biller, F., 373(62), 378
Binder, H. J., 71(70), 79
Bird, H. R., 6(44), 24
Blackburn, R., 346(185), 355
Blackwell, C M., 264(5, 9), 265(5, 9, 13),
266(9), 268(9), 286
Blaisdell,S. J., 70(59), 79
Blakley, R. L., 308(1), 309(1), 342(1), 348,
383(5, 10, 15), 384(5, 10, 15), 385(47,
49), 386(5, 47, 49, 55), 387(49, 62, 63,
64, 65, 66), 388(66), 390(49, 66), 392
(5, 49, 55, 63, 65), 393(49, 55, 83), 394
(49, 55, 61, 63, 65, 83, 85), 395(49, 65),
396(49, 65, 75), 397(49, 63, 65, 86, 87),
398(65), 399(49, 89), 400(49, 90, 91),
401(91), 402(96, 98, 100), 403(96), 404
(100, 103, 104), 405(65, 104), 406(86,
90,91, 105, 106, 107), 407(86, 108, 109),
408(65,90, 108), 409(87, 91, 100), 410
(85, 106), 412(90, 91), 415, 416, 417,
418
Blaschkowski, H. P., 181(111), 201
Blaser,H.U., 128(32), 148
Bloomfield, F. J., 15(154), 28
Boddy, K., 20(205), 30
Bohman,T.,71(64), 79
Bok, J., 22(220), 30
Bolton, F. G., 95(71), 97(71), 103
Bonetti, V., 372(60), 378
Bonnet, R., 334(87), 351
Boretti , G., 5(21), 23
Borodulina-Shvets, V. I., 91(40),
102
Boroush, M. A., 345(164), 354
Borth, R., 89(27),/07
Boutwell, J. H., 89(27), 101
Bowyer, R.C., 89(27), 101
Boyd, D. H., 48(57), 54
Boyer, P. D., 309(25), 337(25), 338(25),
341(25), 349
Bozdech, J. M., 406(107), 418
Bozian,R.C, 12(136), 13(136), 27, 71
(66), 79
Bradbeer, C, 4(16), 33(4, 6), 35(6, 11,16,
42), 36(6, 11, 17, 18), 37(11, 17, 18), 38
(18), 39(29), 40(11, 16), 41(37), 42(40,
41, 42), 43(6, 42, 46), 44(42), 51(85),
52, 53, 54, 55, 93(107), 104, 230(56),
232, 264(1, 2), 286
Bradshaw, W. H., 174(70), 200
Braekkan j O. R., 9(87), 26
Braman,R., 161(48), 164
Brand, M., 74(143), 82
Branden, C-1., 385(43), 416
Brandt, L. J., 94(54), 102
Branion,H.D., 11(116), 26
Braun, I .,5(29),24
Braun,M., 168(19), 198
Braun, V., 47(51), 54
Bray, R. C, 7(63), 11(123), 25, 27, 221
(34), 257
Brewer, J. M., 173(62), 174(73, 74, 77),
175(62, 77), 199, 200
Brinckman, F. E., 161(46), 164
Brink, J. J., 6(38), 24
Brink, N. G., 16(165), 28
Brinkley, S. A., 402(96), 403(96), 417
Britt, R. P., 95(71), 97(71), 103
Brodie, J. D., 287, 320(71), 339(71),
342(133, 134), 351, 353, 371(44), 378
Broitman, S. A., 35(12), 48(12), 52
Brot, N., 182(113), 201, 314(43), 320(73),
350, 351
Broughton, A., 97(66), 102
Broughton, P. M. G., 89(27), 101
Brown, A., 169(
27), 17 3(27), 1 75(27),
195(27), 198
Brown, D. G., 267(20), 282(20), 286
Brown , F., 10(99), 26
Brown, J., 71(94), 80
Brown, J. P., 318(67), 345(169), 351, 354
Brown, M.S., 74(159), 83
Brown, R. L., 91(41), 102
Brown, S. S., 339(112), 340(112), 352
Brownson, C, 385(49), 386(49)
, 387(49),
390(49), 39 2(49), 393(49), 394(
49, 85),
(49), 402
359(49), 3 97(49), 399(49), 400
(98), 404(10 3,104), 405(104 ), 410(85),
416, 417(79), 418
Brownstein, A. M., 234(4), 243(38), 256
(4), 259, 260
Bruckner, H. W., 156(23), 163
Brunfeldt, K., 85(222)
Brunton s L., 21(209), 30
Brzechwa-Ajdukiewicz, A., 98(78), 103
Buchanan, J., 344(154), 354
Buchanan, J. M., 308(5), 309(11,12, 17,
19, 29), 311(42), 314(42), 317(17, 53,
54), 318(12, 63), 319(27), 320(27),
322(54), 327(27), 328(17, 54), 329(17,
29), 336(27), 337(42), 339(53, 110),
340(54), 341(110), 342(42, 110), 349
(19), 350, 351, 352
Buchanan, J. W., 88(23), 95(23), 97(23),
101
Bucher, D., 62(2 11, 212 , 214) , 66(43,
70(43),
45), 67(43 , 45, 221), 69(43),
78, 79, 84, 85
Buckel, W., 372(58), 378
Bucklers, L., 373(63), 378
Buehring, K. U., 345(170), 354
Buettner, G. R., 409(111), 418
Bukin , V. N., 171(53, 54), 199
Bunge,M. B., 95(56), 102
Burger, R. L., 14(151, 153), 15(160), 28, 58
(2) , 61(2), 64(44, 218, 219), 66(44),
70(53), 71(89), 72(89), 74(142), 76
(189), 77, 79, 80, 82, 84, 55,96(112),
104, 363(22), 377
Burgi, H. B., 376(73), 379
Burke, G. T., 342(133, 134), 353
Burkholder, L. M., 6(33), 8(33), 24, 25
Burkholder, P. R., 6(33), 7(49), 8(33),
24,25
Burman, J. F., 73(126), 74(126), 81, 88
(3) , 92(3), 700, 345(183), 355
Burnham, B. F., 144(55), 145(55), 149
Burton, M. O., 9(89), 26
Buschbaum, P. A., 97(62), 102
Bush, P., 50(75), 55
Biitle, R., 73(138), S2
Buttner , J., 89(27), 101
Buxton , R. S., 40(30), 53
Cagen,L.M.,5(15),7(15),25
Callender, S. T., 98(92), 103
Canellos, G. P., 73(123), 74(123), 81,
98(98), 103
Cannata, J. J. B., 360(10), 364(10), 365
(10), 366(10), 367(10), 377
Cannon, J. R., 37(20), 53
Cape, R. D. T., 98(79), 103
Cardinale, G. J., 359(6), 370(43), 376,
378
Cardon, B. P., 171(45, 46, 47), 199
Carlucci, A. F., 8(86), 26
Carmel, R., 15(162), 20(196, 201, 203),
28, 29, 30, 70(52, 54), 73(52, 128,197),
75(52, 166, 171, 174), 76(128, 197,
203, 204), 79, 81, 83, 84, 95(113), 98
(77, 95), 103,104, 140(48), 141(48),
148
Carson , S.F.,368(32),377
Carter,J.E.,194(133),202
Carty, T. J., 244(45), 260, 269(23), 272
(23, 33, 37), 273(37), 278(33), 283
(33), 286, 287
Cary,C. A., 6(42), 24
Cashmore, A. R., 342(135), 353
Castle, W. B., 58(15), 78
Castro, A., 97(62), 102
Cathou, R. E., 309(11, 12, 19), 318(12),
349
Causeley,D.,50(75),55
Cauthen, S. E., 339(98, 99), 352
Cavalli-Sforza, L. L., 73(137), 82
Cederbaum, S., 230(54), 232
Chaikoff,!. L., 358(2), 576
Challenger, F., 151(2, 3), 152(3), 162
Chalmers, J. N. M., 20(206), 30
Chalmers, D. M., 71(69), 79
Chambers, D. A., 257(98), 262
Champion, A. B., 195(144), 202
Chan, Y. K., 161(49), 164
Chanarin, I., 14(150), 15(150), 28, 58(14),
71(69), 72(14, 102), 73(14, 102, 129),
77, 79, 81, 82, 345(175, 176), 346(186,
188), 354,355
Chang, G. W., 264(4), 286
Chang, J. T., 264(4), 286
Chang, S., 98(81), 103
Chaouat, M., 73(135), 52
Charbonneau, L., 152(8), 154(8), 162
Chassey, B. M., 403(97), 418
Chau,M.S., 158(38), 163
Chauser, E. G., 161(52), 164
Cheh, A., 153(13), 162
Cheldelin, V. H., 291(9), 304
Chello, P. L., 342(135), 347(191), 353,
355
Chen, A. K., 386(60), 387(60), 389(60),
392(60), 394(60), 395(60), 397(60),
405(60), 416
Chen, B., 257(97), 262
Chen 5 M. F., 93(50), 102
Cheng, F. W., 342(132), 353
Childs,J. D., 322(75), 351
Chinard, F. P., 212(29), 231
Chirpich,T.P.,2O5(8),250
Chosy,J. J., 385(33), 415
Chow, B. F., 48(56), 54
Chow, R. C, 12(129), 27
Christensen, J. M., 54(210), 90(110), 95
(110), 104
Chu, F., 343(147), 347(147), 353
Cid, A., 97(62), 102, 376(70), 379
Cioffari, A., 376(70), 379
Clark, B. R., 158(34), 163, 310(30), 342
(140), 343(147), 347(147), 349, 353
Clark,H.G.M., 14(150), 15(150), 28
Clark, J. E., 175(87), 176(87), 200
Clark, J. M., Jr., 368(33, 34), 377
Clark, L., 97(62), 102
Clark, M. J., 298(29), 300(29), 301(29),
304
Clark, M. Y., 371(49), 372(49), 378
Coates, M. E., 88(4), 700
Cocking, E. C, 229(49), 232
Cockle, S. A., 245(50), 261
Coffey, J. W., 74( 147), 82
Coffman, R. E., 397(87), 407(109), 409
(87,I I I ) , 417,418
Cohen, C C, 156(23), 163
Cohen , R., 18(180), 29
Cohen, S. S., 2(1), 23
Cohen, W., 72(113), 73(113), 81
Cohn,E. J., 6(41), 24
Cole,T. W., Jr., 363(24), 377
Collings, L., 99(101), 104
Colman, N., 89(32), 96(36), 98(87), 101,
103
Coltman , C A., 95(113), 104
Condon , G., 12(129), 27
Conley, C L., 71(85), 80
Connellan , J., 394(85), 410(85), 417
Cooper, B. A., 21(209), 30, 71(88), 72(88,
103, 110), 73(110), 74(149), 80, 81, 82,
88(14), 98(91), 101, 103
Cooper, M., 344(160), 345(160), 354
Cooper, N. J., 245(56), 246(56), 261
Corcoran , J. W., 7(62), 25
Cords, F., 5(12), 23
Corey, E. J., 245(56), 246(56), 261
Cornforth, J. W., 372(51, 58), 378
Costilow, R. N., 205(5, 8), 223(5), 224
(42), 225(43), 226(43), 230(5), 230,
231
Cotter, R., 61(32), 71(83), 72(101, 104,
105), 73(101), 78, 80, 81
Coulton , J. W., 47(51), 54
Coward, J. K., 342(135), 345(182), 347
(182), 353, 355
Cowey , C B., 8(72), 25
Cowles , J. R., 9(92), 26, 384(17, 27), 386
(17, 27), 388(27), 390(27), 391(17),
392(27), 393(27), 415
Coy , U., 371(47), 378
Craig, G.C, 343(145), 353
Cramer, W. A., 39(25), 53
Cravitz , L., 12(128), 27
Critz, W. J., 402(96), 403(96), 417
Cross, M. J., 10(106), 26, 308(6), 309(6),
349
Cullen, W. F., 151(4), 152(4), 162
Cullen, W. R., 152(5), 162
Culli, A. C, 95(71), 97(71), 103
Curington,C. W., 71(79), 50
Cushley, R. J., 144(51), 148
Cuthbertson, W. F. J., 10(99), 26
Daiger , S. P., 73(137), 82
Daisley,K. W., 8(82), 25
Daniel, L. J., 50(79, 81), 55, 339(100),
352
Darby, W. J., 12(136), 13(136), 27, 71(66),
79
D'Ari Straus, L., 176(79), 200
Davidson, G. E., 345(169), 354
Davies, M. E., 12(127), 27
Davies,M. K., 4(11), 25
Davies, S. P., 245(50), 261
Davis, B. D., 7(48), 10(48), 24
Davis, R. L., 48(56), 54
Dawbarn,M. C, 12(130, 133), 27
Deacon, R., 346(186, 188), 355
De Angelis, L. M., 342(135), 353
Decker, K., 2(6), 23, 32(1), 52
de Crombrugghe, B., 257(97), 262
Deeg, R., 144(52), 148
Degani, Y., 91(46), 102
Dehority, B. A., 11(111), 26
Dekker, E. E., 207(15), 213(15), 231
de Leon, A., 71(95), 80
Deley, J., 2(7), 23
DeUweg, H., 5(20), 23
Deppe, G., 156(23), 163
De Simone, R. E., 152(8), 154(8), 162
Dev, I. K., 176(83), 200
Devaguet, A., 376(73), 379
DeVries, J. A., 22(220), 30, 95(115),
104
Dickerman, H., 309(18), 310(18, 31),
313(41), 320(18, 31), 329(18), 339
(18, 107, 111), 340(18, 111), 341
(111), 349, 350,352
Dickinson, A. B., 5(13), 23
Diekert, G. B., 186(120, 121), 201
Dieterle,W., 191(125), 202
Dietrich, M. R., 15(161), 28
Di Girolamo, P. M., 33(6), 35(6, 11),
36(6, 11), 37(11), 40(11), 42(40),
43(6), 52, 53, 74(152), 82, 317(61),
334(61), 337(61), 338(61), 343(61),
350, 386(61), 390(61), 401(61), 416
Dignam, C T., 93(51), 102
Dilworth, M. J., 309(23), 317(
23), 320
(72), 329(23) , 33 9(72),
(23, 72), 322
349, 351
DiMarco, A., 5(21), 23
Di Masi , D. R., 36(18)
, 3 7(18), 38(18) ,
39(29), 41(37), 53, 93(107), 104
Dinglinger, F ., 5(29), 24, 108(13), 121
(13), 147
Dinning, J. S., 383(7), 415
Dizikes, L. J., 152(12), 153(13), 155
(17), 15 6(17), 1 61(12, 1 7), 162, 163
Diziol, P., 269(27), 270(27), 272(27),
281(27), 286
Dockal,E. R., 158(37), 163
Dohmann, U., 73(125), 74(125), 81
Dolphin, D., 280(53), 281(53), 287, 299
(35), 301(35), 302(35), 304
Donaldson, K. O., 309(14), 318(66), 349,
351
Donaldson, R. M., 68(48), 71(62, 70, 78,
99), 72(114), 73(99, 174), 74(143),
79, 80, 81,82, 93(125), 104
Doran, B. M., 13(144), 27
Doscherholmen, A., 97(67), 98(81), 102,
103
Dowd, P., 374(65, 69), 379
Down, M. C, 14(150), 15(150), 28, 99
(101), 104
Downing, M., 383(14), 384(14), 389(14),
415
Drake, H. L
., 1 83(116, 117) , 1 84(116,
117), 186(118 , 119), 187(121 a), 189
(119,121a), 190(116,119), 201, 202
Dresow, B., 106(3, 4), 109(3, 4, 16), 110
(4), 111(4), 112(4), 114(3,4), 117
(3, 4), 121(3, 4, 16), 122(3, 4, 26, 27,
28, 29), 123(3, 4, 16, 30), 125(3, 16),
126(16), 131(26, 38), 135(4), 138(4),
145(3,4, 16), 147,148
Dreyer, W. J., 296(22), 304
Dreyfus, P. M., 339(119), 352
Droop, M. R., 8(76, 79, 80), 25, 50(70),
54
Dryden, L. P., 6(42), 24
Dunstone, J. R., 387(63), 392(63), 394
(63), 397(63), 416
Duraiswami, S., 383(12), 384(12), 386
(12), 415
Durham, W. R., 245(51), 261, 275(42),
287, 409(112), 418
Du Vigneaud, V., 308(2), 342(2), 348
Dyer, J. K., 205(5), 223(5), 224(42),
230(5), 230, 231
Eagar, R. G., Jr ., 238 (17), 239(1 7, 20) ,
259, 260,
300
240(17), 2 43(17, 20),
(37), 305
Ebersole, E. R., 71(78), 80
Eckstein, F., 388(67), 417
Edenharder, R., 205(10), 230
Edmond, E. D., 112(23), 131(23),
147
Eggerer, H., 301(39), 305, 358(5), 367
(5, 29), 372(58), J76, 377, 378
Ehhalt, D. H., 166(1), 197
Ehrenberg, A., 413(123), 418
Einy-Gorodischer, S., 72(113), 73(113),
81
Eisenberg, L., 76(204), 84
Eisenstein, O., 376(73), 379
Eittoun,R., 76(209), 84
Ekins, R. P., 88(5), 100
Elford, H. L., 317(53, 54), 322(54), 328
(54), 339(53, 110), 340(54), 341(110),
342(110), 350,352
El Ghazzawi, E., 168(22), 169(22), 174
(68), 198, 200
Ellenbogen, L., 58(7), 77
EUiot, J. M., 16(170), 28
Elsden, S. R., 168(24), 170(24), 198
Elsenhans, B., 128(34, 35), 129(34, 35),
130(34, 35), 133(34), 135(34), 139(34),
143(50), 148
Endres 5 D. B., 95(116), 104
England, J. M., 73(129), 82, 99(101), 104
England, M. M., 14(150), 15(150), 28
Engstrom, N. E., 385(37), 416
Epstein,O., 71(71), 79
Epstein, S. S., 50(75), 55
Erbe, R., 342(141), 353
Erbe, R. W., 343(143a), 344(148, 149,
151), 353,354
Erfle,J.D., 368(33, 34), 377
Ericksson 5 S., 383(31), 415
Ernst, L., 109(16), 121(16), 122(28, 29),
123(161), 125(16), 126(16), 131(38),
147,148
Ertel, R., 314(43), 350
Eschenmoser, A., 106(2), 112(2, 19, 21),
131(21), 146,147
Espenson, J. H., 155(18), 156(18, 21),
163
Essenberg, M, K., 236(12), 243(12, 41, 44),
244(12, 41), 259, 260, 271(31), 278(46),
287, 370(41), 378
Evans, H. J., 9(91, 92, 96, 97), 26, 384(17,
27), 386(17, 27), 388(27), 390(27), 391
(17), 392(27), 393(27), 415
Faber 5 J. G., 22(220), 30
Fairwell,T., 174(73), 200
Fanchiang, Y.-T., 152(11), 157(27, 28),
158(36), 159(28), 160(40), 162,163
Farquharson, J., 13(145), 27,88(20), 101
Fasella, P. M., 220(33), 231
Fay, F. S., 51(83), 55
Fedyanin, A. S., 5(14), 23
Fee, J. A., 245(49, 51), 261, 275(42), 287,
301(44), 305, 409(112), 418
Feller, W., 383(30), 415
Fenton, W. A., 99(102), 104, 341(130),
353
Fernandes-Costa, F., 75(178), 83
Fiedler-Nagy, C, 74(147), 82
Fielding, L. P., 71(69), 79
Finalay, T. H., 240(27), 244(27), 260
Finkel,S. I., 403(97), 418
Finkelstein, J. D., 340(121, 124, 125),
341(121, 124, 127,128), 352, 353
Finkler, A. E., 14(146,148,149), 19(186),
20(149, 189, 190), 28, 29, 58(16), 76
(199), 78, 84
Finlay, T. H., 245(47), 261, 301(43), 305
Firkin, B. G., 344(157, 160), 345(160),
354
Firth, J., 12(131), 27
Firth, R. A., 315(45), 350
Fischer, F., 167(12), 198
Fischli, A., 112(21), 131(21), 147
Flaks, J. G., 359(6), 376
Flavin, M., 17(171), 28, 358(1, 4), 376
Fleischer, E. B., 128(33), 131(33), 148
Fleming, A. F., 98(77), 103
Flohr, H., 374(64, 66), 379
Focesi, A., Jr., 360(10), 364(10), 365(10),
366(10), 367(10), J77
Fogg, G. E., 10(99), 26
Folkers, K., 16(165), 28
Follmann, H., 383(30), 385(34), 402
(93, 94, 95), 403(93, 94, 95), 404(93,
(94, 95), 409(113), 415, 417, 418
Fontaine, F. E., 168(21), 169(21), 198
Forage, R. G., 254(90), 255(90), 262
Ford, J. E., 5(19), 9(90), 10(100, 108),
12(125, 132), 23, 26, 27, 50(72), 51(72),
52(72), 54, 88(4), 100
Foss 5 O. P., 71(64), 79
Foster, M. A., 11(122), 27, 33(3), 52, 245
(50, 90), 255(90), 261, 262, 308(9,10),
309(15, 23), 317(23), 320(23), 329(23),
339(98), 349, 352
Fountowlakis, M., 374(67), 379
Fox, J. A., 269(24), 270(24), 275(24),
281(24), 282(24), 286
Francia, M. D., 155(19), 156(19), 160(19),
163
Francis, G . L., 61(36),
78
Franklin , A. L., 7(51), 24
Frank, O., 11(120), 27, 88(24), 97(24),
101
Franzen, J. S., 386(60), 387(60), 389
(60, 74), 392(60), 394(84), 395(60),
396(60), 397(60, 84), 405(60), 410
(84), 416, 417
Frater-Schroder, M., 20(197), 29, 73
(138), 74(139), 75(167, 179), 82, 83
Fredericq, P., 39(27), 40(27), 53
Freedman, D. S., 318(67), 351
Frenkel, E. P., 91(43), 95(108), 97(43),
102, 104
Frey, P. A., 235(12), 238(18), 239(18,
23), 240(26), 243(12, 18, 23, 41, 42,
43), 244(12, 26, 41), 259, 260, 211
(31), 272(34), 278(46), 287, 298(32,
33), 299(32, 33), 304, 370(40, 41),
372(54), 378
Frick, T., 155(19), 156(19), 160(19), 163
Friedman, H. C, 5(15, 17, 25, 26), 7
(15), 23, 24, 205(6), 223(6), 225(6),
230(6), 230
Friedman, J., 309(20), 349
Friedman, P. A., 74(151), 82
Friedman, S ., 3 09(15), 320(72) , 322(72) ,
339(72), 349, 351
Friedner,S.,97(70),;O?
Friedrich, W., 6(36), 7(52), 24, 58(4), 77,
91(39), 92(39), 101, 138(40, 41), 139
(41, 45), 148, 248(67), 261
Fritz, H. L., 156(21), 163
Froese,C. L., 152(5), 162
Fu, M. L, 35(11), 36(1 1), 37(11), 40(11 ),
52
Fuentes, R., 37(22), 53
Fujii, K., 310(34), 311(34), 312(34), 314
(34), 317(34, 60, 61), 318(34, 60, 61),
334(34, 61, 88), 337(60, 61, 88), 338
(61, 88), 339(102), 342(34), 343(61),
347(192), 350, 351, 352, 355
Fukui, S., 6(32), 24, 37(19), 53, 107(9),
109(9), 147, 219(31), 231, 235(7,8,11),
236(11, 13, 14, 15, 16), 237(11, 14, 15),
238(7, 11), 239(7, 19), 240(7, 24), 241
(13, 28, 29, 30, 31), 242(13, 14, 15,
28, 31), 243(19), 244(8, 24), 246(13, 28,
30, 31), 247(15, 57, 58, 62), 248(8, 63,
68, 70), 249(8, 70, 71), 251(8, 70, 74,
76, 77), 252(76), 253(76), 254(88, 89),
255(89, 91), 256(89, 92), 257(88, 89, 91,
101), 258(101, 102), 259, 260, 261, 262,
296(24), 304, 337(93), 339(101, 104,
106), 352
Fyfe, J. A., 5(26), 24
Galivan, J., 311(38), 312(38), 317(38),
350
Galivan, J. H., 317(60), 318(60), 337(60)
350
Gallagher, N., 71(94), 80
Gallagher, N. D., 71(96), 80
Galloway 5 E., 339(113), 352
Gams, R. A., 74(150, 156), 75(177), 82,
83
Gardiner, W., 385(49), 386(49), 387(49),
390(49), 392(49), 393(49), 394(49), '
395(49), 396(49), 397(49), 399(49),'
400(49), 416
Garibaldi, J. A., 11(115), 26
Gartha, S., 21(209), J0
Gaston, L. W., 167(16), 198
Gathorne, J. M., 345(174), 354
Gerhardt,P.,49(59),54
Genloff,G.C, 10(101), 26
Gerwin, B. I., 362(19), 364(19), 377
Ghambeer, R. K., 176(92), 177(92), 178
(106), 179(106, 108), 180(108), 182
(92), 189(106), 201, 383(15, 28), 384
(15), 399(89), 402(98, 100), 404(100,
103, 104), 405(104), 415, 417, 418
Ghione, M., 5(21), 23
Ghoi,G., 15(161), 28
Giannella, R. A., 35(12), 48(12), 52
Gibson, F., 308(3), 309(3), 349
Gilbert, H., 75(180), 83
Gilbert, H. S., 20(198, 200), 29, 64(219),
75(163, 183), 76(183, 191), 83, 84, 85
Giles, C, 98(85), 103
Gillard,R. D., 158(31), 163
Gimpert, E., 73(129), 74(127), 81, 98(97),
103
Gimsing, G., 95(126), 104
Gimsing, P., 20(199), 29, 72(117), 75
(187, 188), 76(193, 205), 81, 84
Girdwood, R. H., 93(49), 102
Gizis, E. J., 15(161), 28
Gj0rup, S., 98(80), 705
Glass, G. B. J., 58(3), 70(3), 71(3, 92),
77, 80,96(117), 104
Gleason, F. K., 10(104), 26, 50(74), 54,
383(18,19, 24, 29), 384(18, 19, 24, 25),
386(18, 19, 24, 25), 388(18), 389(29),
390(18), 391(19, 24, 25, 80), 392(18),
398(18), 399(18), 404(18), 405(18),
415, 417
Gneuss, K. D., 144(52), 148
Goldberg, E. D., 161(45, 47), 164
Golding, B. T., 376(72), 379
Goldstein, J. L., 74(159), 83
Golenko,0. D., 158(35), 163
Goodman, S. I., 21(211), 22(211), 30
Gordin, R., 72(112), 73(112), 81
Gosio 5 B., 151(1), 162
Gottesman, M., 257(97), 262, 402(99),
404(99), 418
Gottlieb, C, 7(59), 25, 97(73), 103
Gottschalk, G., 167(9), 168(9, 19), 169
(9), 170(9, 35), 174(68), 198,199, 200
Gottwald, M., 170(34), 196(34), 198
Gould, D. C, 223(40), 231, 274(39, 40),
287, 301(41), 305
Gould, J. M., 34(25), 47(53), 53,
54
Goulian, M., 385(48), 386(48, 58, 59),
387(59), 389(48), 392(48), 393(48,
59), 416
Grabbe, E. E., 71(84), 80
Graf, E.G., 186(121), 201
Granser, E. G., 158(32), 163
Grant, M. A., 207(18), 231
Grant, M . E ., 3 7(22), 53, 313(40), 350,
400(92), 401(92), 417
Grasbeck, R., 13(139), 20(192), 27, 29,
58(8, 13), 59(18, 19, 20, 21, 22), 61
(35), 65(13), 70(58), 71(13, 74, 75,
76, 77, 97), 72(97, 106, 108, 109,
112), 77, 78, 79, 80, 81, 88(12), 96
(120), 98(88), 700, 70.?, 104
Graslund, A., 413(123), 418
Graves, S. W., 269(24, 27), 270(24, 27,
29), 272(27), 276(24), 280(29), 281
(24, 27, 29), 282(24), 286, 287
Green, M. L. H., 245(56), 246(56), 261
Green, P. A., 73(134), 82
Green, P. D., 73(130), 74(145,161),
82, 83
Green, R., 95(69, 111), 97(69), 98(87),
103,104
Greene, R. C, 322(77), 351
Gregory, M. E., 4(11), 13(144), 23, 27
Griffin, C E., 406(101), 418
Griffiths, J. M., 50(79), 55, 339(100), 352
Grob, P. J., 20(197), 29, 75(167), 83
Grobner, P., 181(111), 201
Grosberg, S., 89(32), 96(32), 101
Groschke, A. C, 6(44), 24
Gross, J., 5(24), 20(191), 29, 75(186), 84
Grossowicz, N., 75(173), 83, 99(100),
104
Grzelakowska-Sztabert, B., 343(146), 353
Guenther, E., 339(105), 352
Guest, J. R., 11(122), 27, 33(3), 52, 308
(6, 10), 309(6, 15, 20), 320(72), 322
(72), 339(72), 349, 351
Gullberg 5 H. S., 76(192), 84
Gullberg, R., 75(182), 55
Gunasegaram, R., 19(183), 29, 95(72),
97(72), 103
Gunsalus, I. C, 192(128), 194(140), 195
(143), 202
Gunther, H., 373(62), 378
Gunzer,G., 144(52), 148
Gusberg,S. B., 156(23), 163
Guterman,S. K., 48(57), 54
Gutschow, C, 372(58), 378
Haas, H., 269(27), 270(27), 272(27), 281
(27), 286
Haas, V., 170(41, 42), 799
Haber, E., 84
Hacking, A. J., 194(137), 202
Hagedorn, C H., 71(91), 72(91), 80
Hakami, N., 73(123, 124), 74(123, 124),
81,98(98), 103
Halbrook,E. R., 5(12), 25
Hall, C A., 12(137), 14(146, 148, 149),
15(156, 157), 19(185), 20(149, 189,
190), 27, 28, 29, 58(16), 64(217), 70
(56, 57), 73(122, 133, 134, 144), 74
(144, 145,161), 75(56, 57,172), 76
(198, 199), 78, 79, 80, 81, 82, 83, 84,
88(15, 19), 91(42), 98(94, 96, 99), 99
(15, 99), 707, 102,103,104
Halpern, B. C., 158(34), 163, 342(140),
343(147), 347(147), 353
Halpern, J., 158(37, 38, 39), 163
Halpern, R. M., 158(34), 163, 310(30),
342(140), 343(147), 347(147), 349, 353
Halsey,M. J., 346(186), 355
Hamilton, F. D., 384(23), 385(51), 386
(23), 388(23), 389(23), 392(23), 398
(23), 399(23), 406(101), 415, 416, 418
Hamilton, J. A., 397(86, 87), 406(86,
105), 407(86), 409(87, 110), 417, 418
Hammond, K. B., 21(211), 22(211), 30
Hanna, M. L., 34(9, 10), 43(10), 45(9), 52,
91(37), 101, 157(26), 160(42), 163,164,
316(48), 317(48, 57), 318(62), 319(69),
321(62), 322(69, 78), 325(79), 326(69),
333(62,86), 337(62), 542(142), 343(142),
345(163, 178, 179, 180), 350, 351, 353,
355
Hansen, I. A., 50(76), 55
Hansen, M. R., 61(38), 62(38), 66(45),
67(45), 68(47), 69(38), 70(38), 78,
79,96(124), 104
Hansen, 0. P., 98(80), 103
Hanson, J., 158(38), 163
Hanssen, K. F., 71(72, 73), 79, 80
Happe, J. A., 157(29), 163
Hardy, D. N., 158(34), 163, 342(140),
343(147), 347(147), 353
Hardy, J., 384(13), 386(13), 389(13),
399(13), 415
Harmony, J. A. K., 176(78), 200
Harris, B. J., 340(121), 341(121,127),
352, 353
Harrison, J. E., 194(136), 202
Hart, A. C, 359(7), 376
Hartman, A. M., 6(42), 24
Harvey, R. J., 176(83), 200
Hatch, F. T., 308(5), 309(19), 318(63),
349, 351
Haurani, F. I., 73(144), 74(139,144),
82, 98(94), 103
Hay, G., 22(216), 30
Hayashi, M., 106(6, 7), 109(6, 7), 147,
248(64, 66), 261, 294(19), 304
Hayward, H. R., 264(7, 8), 286
Heath, C W., 58(15), 78
Hedges, A. J., 40(33), 53
Heinrich, H. C, 71(84), 80, 139(45),
148, 248(67), 261
Helinski,D. R., 39(28), 53
HeUeiner, C W., 308(4, 6), 309(6), 349
Heppel, L. A., 34(7), 45(49), 52, 54
Herbert, V., 7(59), 15(154, 162), 25, 28,
70(53), 73(197), 75(175,176), 76(195,
197), 79, 83, 84, 89(32, 33), 96(32),
97(73), 98(95), 101,103, 141(49),
148, 344(153,154, 156),354
Herbst, M. M., 300(37), 305
Herrmann, H., 339(105), 352
Herschman, H. R., 39(28), 53
Hersh, L. B., 194(134,135), 202
Hervey, A., 8(71), 25
Heyssel, R. M., 12(136), 13(136), 27,
71(66), 79
Hiei, E., 59(26), 78, 310(32), 311(32),
320(32), 349
Hildebrand, R., 93(106), 104, 247(61),
261
Hill, H. A. O., 152(8), 154(8), 155(16),
156(16), 157(25, 30), 159(25), 162,
163, 245(50), 261, 315(45), 350
Himes, R. H., 176(78), 200
Hinds, K. R., 342(137), 353
Hine,D. C, 12(130,133), 27
Hippe, E., 20(199), 29, 68(46), 72(116,
117), 76(205), 79, 81, 84(210), 85,
95(60,114), 97(60), 98(80), 102,103,
104
Hitzig, W. H., 20(197),
29, 73(125,127,
138), 74(125 ,127, 139,160 , 161) , 75
(167,179), 81, 82, 83, 98(97), 103
Hjelt,K., 72(115,116), 81
Hodge, V. F., 161(47), 164
Hodgkin, D. C, 37(23),
53, 112(23), 131
(23), 147
Hoedemacker, P. J., 71(61), 79
Hoffbradn, A. V., 161(53), 164
Hoffbrand, A. V., 20(195), 29, 72(100,
102), 73(102 ), 7 5(164,196), 80, 81, 83,
84, 97(61), 99(105), 102,104, 345(171,
173,177), 354,355
Hoffmann, C E., 7(51), 24
Hoffmann, P.
J., 381(64), 400( 91), 401
(91), 406 (91), 4 09(91), 4 12(91), 416,
417
Hoffmann, R., 376(71), 379
Hoffman, R. M., 344(148,149,151), 354
Hogenkamp, H. P. C, 11(113), 26, 37(22,
24), 50(74), 53, 55, 59(25), 78, 139(42),
148, 235(8), 244(8), 247(58, 62a), 248
(8), 249(8, 72), 251(8), 259, 261, 294
(21), 304, 313(40), 314(44), 315(47),
328(83), 337(91), 350, 351, 383(18,19),
384(18,19, 21, 26), 386(18,19, 21, 26),
388(18,21,26, 68), 390(18, 21), 391(19,
80), 392(18, 21), 393(21, 26), 394(85),
397(86), 398(18, 21, 26), 399(18, 21,
26), 400(21, 91, 92), 401(92), 402(93),
403(93), 404(18, 21, 26, 93,103,104),
405(18, 26,104), 406(86, 91), 407
(86), 409(56, 91,113), 410(85), 412
(56, 91,119), 415, 416, 417(79), 418
Holdeman, L. V., 170(40), 199
Holdsworth, E. S., 5(19), 12(125), 23, 27
Hollaender, N., 72(117), 81
Holland, I. B., 35(45), 43(45), 53
Holland, J. F., 156(23), i65
Holland, R. J., 278(44),
287, 410(115,
117), 411(117), 418
Hollander, D., 20(196), 29, 75(166), 83
Hollaus, F., 170(36), 199
, 274 (25), 27 5
Hollaway, M. R., 269(25)
(25), 276(25), 283(25), 286
Holldorf, A. W., 337(90), 351
Hollenberg, M. D., 74(146), 82
Holmes, S., 337(91 ),351
Holmgren, A., 385(36, 37, 38, 39, 40, 41,
42, 43, 44, 45, 52), 415, 416
Holm-Hansen, O., 10(101), 26
Holmquist, B., 283(57), 284(57), 287
Holzer, H., 257(99), 262
Horn, B., 75(169), 83
Horn, B. L., 15(155, 159, 163), 20(16 3),
28, 70(51), 73(168), 74(141), 75(168),
78, 82, 83, 98(93), 103
Honda, S., 255(91), 256(92), 257(91, 101),
258(101), 262
Hong, J. S., 47(55), 54
Hook, S., 386(57), 416
Hook, S. A., 11(119), 27
Hooper, D. C, 71(89), 72(89), 80
Hoover, S. R., 6(35), 24
Hopner, Tk., 205(10), 230
Hopper, S., 386(60), 387(60), 389(60),
392(60), 394(60), 395(60), 396(60),
397(60), 405(60), 406(101), 416,
418
Hosoi, N., 256(93), 262
Houlihan, C M., 345(168), 354
Hsieh, P., 345(182), 347(182), 355
Hsu, J. M., 13(140), 27
Hu, S. I., 183(116, 117), 184(116, 117),
186(118, 119), 187(121a), 189(119,
121a), 190(116, 119), 201, 202
Huber, F., 161(50, 51), 164
Huennekens, F. M., 74(152), 82, 310(34),
311(34, 38), 312(34, 38), 314(34), 317
(34, 38, 60, 61), 318(34, 60), 320(71),
334(61), 336(88), 337(34, 61), 338(61),
339(71), 342(34), 343(61), 350, 351, 386
(61, 153), 389(53), 390(61), 393(53),
401(61), 416
Huff, J. W., 382(2), 386(2), 414
Hughes, A., 72(102), 73(102), 81
Hull, W. E., 266(17), 283(17, 56), 286,
287
Hume, R., 22(215), 30
Hummel, J. P., 296(22), 304
Hungate, R. E., 167(15), 198
Hunt, A. G., 47(55), 54
HurUman , J., 75(185), 83
Hussein, H. A.-A., 7(57), 25, 88(21),
101
Hutner, S. H., 7(51), 9(90), 10(100), 11
(120), 24, 26,27, 51(84), 55
Hutton , J. J., 345(163), 354
Hyman , M. P., 76(207), 84
Ichikawa, Y., 256(93), 262
Ijichi,K., 11(115), 26
Ikeda,H.,7(50),24
Ikeda 5 K., 7(64), 25
Immerslund, O., 72(111), 73(111), 81
Ingraham, L. L., 180(110), 201, 301 (40), 305
Inukai, S., 9(93), 26, 339(103), 352
Iodice, A. A., 230(53), 232, 291(10),
292(16), 293(10), 295(10), 297(27),
298(16), 304
Irion, E., 176(91), 177(91, 96, 97, 98),
178(91, 96), 179(91, 96, 109), 180
(91), 190(96, 98), 191(96, 97, 98),
201, 279(51),257
Isaacs, J. D., 8(84), 25
Isemura, Y., 236(13), 241(13), 242(13),
246(13), 259
Ishikawa, Y., 407(109), 418
Ithakissios, D. S., 95(63), 97(63), 102
Izumi, Y., 140(47), 141(47), 148
Jablin,K. N., 265(10), 286
Jackson, W. R., 315(45), 350
Jacob, E., 70(53), 72(121), 75(175,176),
79, 81,83, 89(33), 101
Jacob 5 F., 12(126), 27
Jakob, M., 98(97), 103
Jacobs, W. L. W., 91(45), 102
Jacobsen, D. W., 59(27), 78, 317(61),
334(62), 337(61), 338(61), 343(61),
350, 386(53, 61), 389(53, 70), 390
(61), 393(53), 401(61), 416, 417
Jacobsen, S. J., 344(149, 151), 354
Jacobson, B., 362(17, 19), 364(19), 377
Jacobson, G., 253(80), 254(80), 262
Jaenicke, L., 17(173), 28, 160(44), 164,
309(26), 310(33, 37), 311(33, 37),
314(33), 317(33, 37, 55), 318(33, 64),
320(33), 328(33), 336(33, 89), 338(26,
55), 343(144), 349, 350, 351, 353
Jakob, M., 73(127), 74(127), 81
James, G. W., III., 22(214), 30
Jandl, J. H., 22(218), 30
Jasewicz, L. B., 6(35), 24
Jeng, 1.-M.,207(17),2i7
Jensen, F. R., 239(21), 260
Jewett,K. L., 161(46), 164
Joblin, K. N., 269(25), 274(25), 275
(25), 276(25), 283(25), 286
Johnson , A. W., 37(20), 53, 130(37), 148,
265(10), 269(14, 25), 274(25), 275(25),
276(25), 283(25), 286, 309(21), 349,
371(45), 378
Johnson, B. C, 12(131), 27, 253(80,
81), 254(80, 81, 85), 262, 368(33, 34),
377
Johnson, J., Jr., 363(24), 377
Johnson, M. J., 168(21), 169(21), 198
Johnson, P. J., 76(206),
Jones, C, 345(180), 355
Jones, E., 363(24), 377
Jones, N. E., 8(75), 25
Jorgensen, J., 18(180), 29
Josephson, B., 97(70), 103
Judglman, J., 71(71), 79
Jukes, T. H., 7(51), 13(143), 24, 27
Jungermann, K., 2(6), 23, 32(1), 52
Kabakow, B., 156(23), 163
Kadner, R. J., 33(6), 35(6, 13, 14), 36
(6, 14, 15), 40(15, 31, 34, 35), 41(35),
42(31), 43(6, 35, 46,47), 44(14), 52,
53, 54
Kahan, D., 51(86), 55
Kajiwara, M., 144(51), 148
Kalamegham, R., 98(86), 103
Kamely, D., 342(141), 344(150), 353,
354
Kamen, M. D., 169(28), 170(42), 198,
199
Kamikubo, T., 5(28), 24, 106(7),
109(7), 147, 248(64, 65, 66), 261,
304(19)
Kane 5 P., 76(206),
Kane, S. P., 20(195), 29, 75(164), 83
Kang, K., 374(68), 379
Kantero, I., 72(112), 73(112), 81
Kao, F.-T., 345(180), 355
Kapadia, C R., 71(78), 72(99), 73(99), 80
Kaplan, B. H., 211(26), 230(26), 231, 264
(3), 265(3, 11), 266(3, 11), 267(3), 268
(3), 286
Karabatsos, G. L., 239(18, 23), 243(18,
23), 259, 260, 372(54), 378
Karlsson, J. L., 167(14), 170(37), 198,199
Karstoft, H., 88(7), 90(7), 91(7), 96(7), 98
(7), 100
Kashket, S., 11(118), 26, 49(60, 61, 62,
63), 54
Kass, L., 58(1), 77, 345(164, 165), 354
Kato, T., 239(19), 243(19), 248(63), 260,
261
Katz, J., 358(2), 376
Katz, M., 61(37), 63(37), 64(37), 71(88,
93, 95), 72(88, 103, 110), 73(110),
78, 80, 81
Katzen, H. M., 317(54), 322(54), 328(54)
340(54), 350
Kaufman, J. T., 11(118), 26, 49(60, 62), 54
Kawamura, H., 240(24), 244(24), 260
Kawasaki, T., 65(40), 78
Kawin 5 B., 13(140), 27
Kaziro, Y., 364(27), 371(27, 48), 372(27),
377, 378
Keller, S., 95(108), 104
Kellerman, G. M., 361(13), 363(13), 365
(13), 366(13), 367(13), 377
Kellermeyer, R. W., 297(25), 304, 359
(9), 361(13, 14), 362(20), 363(13),
364(20), 365(13), 364(20), 366(13),
368(31), 377
Kellner, M., 373(62), 378
Kelly, A., 141(49), 148, 344(156), 354
Kempe, U. M., 374(64), 379
Kenley, J. S., 36(17, 18), 37(17, 18), 38
(18), 41(37), 52, 53, 93(107), 104
Kennedy, E. H., 20(204), 22(215), 30
Kennedy, F. S., 152(6), 155(16), 156(16),
162,163, 177(94), 201
Kenny, A. B., 20(197), 29, 74(160), 75
(167, 179), 83
Keresztesy, J. C, 309(14), 316(66), 349,
351
Kersters, K., 2(7), 23
Kerwar, S. S., 243(43, 44), 249(73), 260,
261, 278(46), 287, 320(71), 339(71),
342(138), 344(150), 351, 353, 354
Khalifah, L. I., 35(16), 40(16), 41(16), 52
Kikuchi,G., 194(141, 142), 195(142), 202
Killander, A., 97(59), 98(83, 84), 102, 103
Killman, S. A., 344(155), 354
Kilpatrick, G. S., 98(82), 103
Kim, J. J., 389(74), 394(84), 397(84), 410
(84), 417
Kim,Y. S., 72(118), 81
King, P., 20(205), 30
King, T. E., 291(9), 304
Kipnes 5 R. S., 283(57), 284(57), 287
Kirchman,H., 161(51), 76
Kirchner, J., 389(70), 41 7
Kirschfeld, S., 383(8), 475
Kirschner, M. W., 398(88), 408(88),
417
Kisliuk, R. L., 11(121), 27, 308(7, 8),
318(65), 339(97), 349, 351, 352
Kissane,J.M.,391(81),4i7
Kitahara, K., 49(64, 65, 66, 67), 54
Kitamoto, Y., 256(93), 262, 345(182),
347(182), 355
Kitay, E., 382(1, 3, 4), 383(4), 386(1, 3,
A), 414, 415
Kitay, J. E., 10(107), 26
Klaassen, C H. L., 22(212), 30
Klebe, H., 7(65), 25
Klee, W. A., 337(94), 352
Klein, S. M., 194(132, 138,139), 202
Kliewer, M., 9(96, 97), 26
Knappe, J., 181(111, 112), 201, 205(10,
I l 1 230
Koch, J., 340(120), 352
Kohn, J., 76(206),
Kolhouse, J. F., 17(175), 18(175, 177),
29, 68(49), 71(49), 74(153), 79, 82,
88(25), 93(57), 95(25, 57), 97(25),
101, 102, 340(122), 352
Kolhouse, J. R., 7(61), 12(61), 17(61), 25
Kon, H., 278(48), 284(48), 287
Kon, S. K., 4(11), 5(19), 10(109), 23,
94(53), 102
Kondo, H., 7(61), 12(61), 17(61, 175), 18
(175), 25, 88(25), 95(25), 97(25), 101
Kondo, M., 236(13, 14), 237(14), 241
(13), 242(13,14), 246(13), 259
Ksnig, A., 361(15), 363(15), 366(28),
367(15), 368(15, 28), 369(15, 28),
370(15), 373(15), 377
Konigk, E., 248(67), 261
Koniuszy,F. R., 16(165), 28
Koppenhagen, V. B., 106(4), 107(10),
108(11, 12, 15), 109(4, 16), 110(4),
111(4), 112(4), 114(4), 115(25), 117
(4, 10), 118(4), 119(4, 10), 120(10, 12),
121(4, 10, 12, 16), 122(4, 26, 27, 28, 29),
123(4, 16, 25, 30), 125(16, 25), 126(10,
12, 16), 128(10, 12, 15, 34), 129(15, 34),
130(34), 131(15, 26, 38), 133(34), 135
(4, 15, 34), 138(4), 139(12, 34,46),
140(48), 141(48), 143(50), 145(4, 16,
58), 747,148,149
Kosuga, T., 235(7), 238(7), 239(7), 240(7),
259
Kouvonen, I., 71(37), 72(37, 109), 80, 81
Kozarich, J. W., 412(121), 418
Krampitz, L. O., 184(121b), 202
Krasma, A. I., 7(69), 25
Krebs, T., 374(64), 379
Krevans, J. R., 71(85), 80
Kriemler, H.-P., 144(52), 148
Krishnaswamy, K., 98(86), 103
Kristensen, H. P. O., 50(77), 55
Kristiansen, K., 62(41), 65(41), 66(41),
67(41), 78, 90(110), 95(110), 104
Krodel, E., 235(9), 244(9), 245(9), 247
(9), 248(9), 259
Kroese,W. F. S., 22(220), 30
Krouwer, J. S., 271(29), 278(47), 279
(50), 280(52), 281(29), 283(52, 57),
284(57), 287, 339(109), 352
Kubiatowicz, D. O., 95(63), 97(63), 102
Kuhlback, B., 72(112), 73(112), 81
Kumamoto, N., 5(28), 24, 248(65), 261
Kung, H. F., 33(5), 52, 230(54), 232,
322(77), 351
Kuno, S., 254(89), 255(89, 91), 256(89),
257(89, 91), 262
Kunz, F., 222(36, 37), 231, 372(56), 378
Kuratomi, K., 177(99, 100, 101), 178(99,
100, 101, 105), 180(100), 181(100), 201
Kurganov, B. I., 91(40), 102
Kurz, W., 362(18), 377
Kutzbach,C, 339(113), 352
Kutznetzova, J. P., 158(35), 163
Kyaw, M., 346(185), 355
Kylc,W. E., 340(121), 341(121, 127), 352,
353
Labowe,M. L., 73(137), 82
Ladd, J. N., 290(6), 299(36), 303, 305
Lakowicz, J. R., 153(13), 162
Landau, L., 89(32), 96(32), 101
Langwell, H., 168(25), 198
Lankhorst, A., 167(17), 198
Lappert, M. F., 265(10), 266(14), 269(25),
274(25),275(25),276(25),283(25),286
Larrabee, A. R., 309(11, 12, 19), 318(12),
344(154), 349, 354
Larsen, E. G., 253(80), 254(80), 262
Larsson, A., 385(37, 48), 386(48), 389
(48), 393(48), 416
Lascelles, J., 5(23), 10(106), 23, 26, 339
(99), 352
Lau, K.-S., 7(59), 25, 97(73), 103
Laundy, M., 345(176), 355
Laurent, T. C, 385(35), 390(77), 415,
417
Lauridsen, L., 98(80), 103
Lavoie, A., 76(196), 345(171, 173,
177), 354
Law, P. Y., 267(20), 282(20), 286
Lawson, D. H., 22(216, 217), 30
Lawson, J., 91(44), 102
Layton, L. L., 48(56), 54
Lazerson, J.,98(98), 103
Lazerson, R. N., 73(123), 74(123), 81
Lear, A. A., 19(181), 22(221), 29, 30
Lecar, H., 278(48), 284(48), 287
Lee, D. A., 7(66), 25
Lee, E., 145(56), 149
Lee, H. A., Jr., 230(55), 232, 234(5),
235(5, 6), 240(5, 26), 241(5), 242
(5), 244(26, 46), 246(5), 248(6),
259, 260, 272(34), 287
Lee, J.P., 190(122), 202
Lee, L., 84
Lee, M. N., 290(4), 291( 4),
303
Lee, S. K., 72(110), 73( 110), 81
Le Gall, J., 170(34), 173(57), 184(57),
190(122), 196(34), 198,199, 202
Leighton, M., 36(17, 18), 37(17, 18),
38(18), 53, 93(107), 104
Lein, E. L., 267(20), 282(20), 286
Lennox, E. S., 42(44), 53
Lentz, K. E., 169(31), 172(31), 198
Lenz, K., 71(90), 80, 171(44), 173(44),
199
Leong, J., 47(52), 54
Letendre 5 C H., 50(81), 55
Levi, A. J.,71(69), 79
Levin, K., 97(70), 103
Levine, J. S., 71(63), 79
Levy, H. L., 21(210), 30, 339(114, 115,
119), 341(129), 342(137), 352, 353
Lewin, R. A., 8(81), 25
Lewis, A., 402(96), 403(96), 417
Lewis, G. P., 347(189), 355
Lewis, J. C 5 11(115), 26
Lexa, D., 160(41), 164, 337(92), 351
Lezius, A. G., 294(18), i04
Li, L.-F., 173(60), 199
Li, T. K., 265(12), 266(12), 267(12), 286
Lieberman, M. A., 47(55), 54
Lien, E. L., 91(36), 101
Lieske 5 R., 167(12), 198
Liggins, G. L., 36(15), 40(15), 52
Likely, G. D., 6(42), 24
Lilljequist, A.-C, 359(8), 376
Lin, P.-F., 344(152), 354
Lindemans, J., 61(28), 62(28, 213), 78,84
Lindstrand, K., 7(55), 16(55), 24, 88(18),
101
Linke,H. A. B., 178(103), 201
Linnell, J. C, 7(56, 57), 16(166), 17(166),
19(56, 166, 182,183, 184), 24, 25, 28,
29, 72(100), 76(194), 80, 84, 88(16, 17,
21), 90(16), 91(16), 95(72), 97(72), 99
(16, 101, 105), 101,103,104, 158(33),
161(53), 163,164, 344(162), 354
Lippard, S. J., 156(22), 163
Littlefield, J. W., 342(141), 353
Liu, C-K., 20(202), 30
Liu, M.-T., 174(76), 176(84, 85), 200
Ljungdahl, L. G., 166(7), 168(18), 169(27)
170(32, 33, 34), 171(33), 172(7, 18, 32, '
55), 173(27, 32, 57, 60, 61, 62, 63), 174
(61, 64, 65a, 66, 72, 73, 74, 75, 76, 77),
175(18, 27, 32, 62, 77, 86, 87), 176(84,'
85, 86, 87, 91, 92), 177(91, 92, 96, 97,'
98), 178(18, 32, 91, 96, 104, 106), 179
(91, 96,106, 108, 109), 180(91, 108),
182(92), 184(57), 189(106), 190(96,
98, 122), 191(96, 97, 98, 124), 192(33),
195(27), 196(33, 34), 198,199, 200, 201
202
Lloyd, D., 50(71), 54
Lochhead, A. G., 9(88, 89), 11(88), 26
Lochmuller, H., 364(25), 377
Lockwood 5 S., 51(84), 55
Long,M. V., 368(32), 377
Looney, F. D., 397(86), 406(86, 105), 407
(86), 417, 418
Loughlin, R. E., 317(53), 339(53,110), 341
(110), 342(110), 350, 352
Lous, P., 21(208), 30, 62(211), 75(169),
83, 84
Low-Beer, T. S
., 98(78 ), 103
Lowenstein, L.,
21(209), 30
Lu,S.-H.,7(68),25
Ludwig, W., 402(94, 95), 403(94, 95), 404
(94, 95), 417
Lui, A., 152(5), 162
Lumb, M., 345(175, 176), 346(186,188),
354, 355
Lund, G., 191(124), 202
Luria, S. E., 39(26), 53
Luthy, J., 372(59), 378
Luthy,R.,74(139),S2
Luxon,P. L., 161(49), 164
Lymn,A. H., 168(25), 198
Lynen, F., 301(39), 305, 358(5), 361
(12), 363(12), 364(25), 365(12), 366
(12), 367(5,12, 29), 368(12), 371(47,
50), 376,377, 378
McAuslan, B., 342(138), 353
McBride, B. C, 151(4), 152(4, 5), 162
McBurney, M. W., 345(143), 353
McCall, M. S., 91(43), 95(108), 97(43),
102,104
McCarthy, C F., 98(78), 103
McClung, L. S., 171(48), 199
McCoy, E., 168(21), 169(21), 198
McDougall, B. M., 317(53), 339(53), 350
McElhaney, G., 43(47), 54
McEwan, F. C, 96(58), 97(58), 102
McGing, P., 346(187), 347(190), 355
McGuire, J. J., 345(182), 347(182), 355
Machlis, L., 50(69), 54
Mclntyre, P. A., 71(85), 80, 88(23), 93
(50), 95(23), 97(23), 101,102
Mackawa, A., 383(11), 415
McKenna, B., 347(190), 355
Mackenzie, H. M., 7(56), 19(56, 182), 24,
29, 76(194), 88(17), 84,101, 344(162),
354
Mackenzie, I. L., 72(114), 73(114), 81
Mackenzie, R. E., 176(80), 200
McLaughlin, J. J. A., 8(76), 25
Macleod, A., 20(205), 30
McMahon, J., 97(67), i02
McNutt, W. S., 10(107), 26, 382(1, 3,4),
383(4), 386(1, 3,4), 414, 415
Magnusen, R. H., 158(39), 163
Mah, R. A., 166(3, 5), 197,198
Mahoney, M. J., 342(139), 353, 359(7),
376
Majerus, P. W., 14(147), 15(147), 28, 58
(2), 61(2, 31), 64(216, 220), 77, 78, 85,
96(112), 104, 363(22), 377
Malahov, A. A., 254(86), 262
Mandal, A. R., 93(51), 102
Mangum, J. H., 309(16), 320(71), 339(16,
71, 116,118), 340(118), 342(116, 118,
133, 134, 136), 349, 351, 352, 353
Manny, N., 76(200), 84
Manson,L. A., 383(9), 415
Mantorani, V., 99(104), 104
Maragoudakis, M. E., 291(9), 304
Marcoullis, G., 61(35), 70(55, 58), 71(74,
75, 76, 82), 72(106, 107, 108), 78, 79,
80, 81, 96(120), 104
Marquet, J., 20(193), 29, 76(201, 208,
209), 84
Marshall, R. A., 22(218), 30
Marston, H. R., 12(135), 27
Martin, B. A., 7(66), 25
Martin, J. J., 341(127), 353
Martinez, D., 8(75), 25
Mason, H. S., 314(44), 350
Masters, P. S., 47(55), 54
Mathan, V. I., 68(48), 72(114), 73(114),
79, 81, 93(125), 104
Mathias, M. M., 16(170), 28
Matsumoto, T., 249(71), 261
Matteuzzi, D., 170(36), 199
Matthews, D. M., 7(56, 57), 16(167), 19(56,
182, 183), 24, 25, 28, 29, 72(100), 76
(194), 80, 84, 88(17, 21), 91(38), 95(72),
97(72), 99(105), 101, 103, 104, 158(33),
161(53), 163, 164, 344(162), 354
Matwiyoff, N. A., 37(22, 24), 53, 247(62a),
261
Mauck, L., 266(17, 18), 283(56), 286, 287
Mayer, F., 174(76), 200
Mazumder, R., 3 60(10, 11) , 361( 11), 364
(10, 11, 26, 27) , 365 (10), 366( 10), 3 67
(10), 371(27,48), 372(27), 377, 378
Meehan, A. M., 64(217), 85
Mehlman, C S., 14(151), 15(160), 28, 58
(2), 61(2, 34, 37), 63(39), 64(34, 37,
215, 218, 219), 67(34), 71(89), 72(89),
74(142), 76(189), 77, 78, 80, 85, 96
(112, 121,122), 104, 363(22),
377
Mellman, I., 341(131), 353
Mellman, I. S., 74(154, 155), 83, 340(123),
344(152), 353, 354
Menkes, H., 151(4), 152(4), 162
Merivuori, H., 71(76), 80
Merkenschlager, M., 362(18), 377
Mervyn, L., 5(27), 24, 20(205), 30, 130
(37), 148, 309(21), 349
Metz, J., 75(178), 83, 98(87), 103, 141
(149), 148, 344(156), 354
Meulengracht, E., 21(208), 30
Meyer, L. M., 15(161), 28, 75(177), 83
Michna, H., 145(59), 148
Mickelson, M. N., 234(2), 259
Migliacci, A., 5(21), 23
Mildvan, A. S., 235(9), 244(9), 245(9,47,
48), 247(9), 248(9), 259, 301(43), 305
Miller, G., 191(125), 202
Miller j L F., 15(161), 28
Miller, I. M., 7(62, 64), 25
Miller, O. N., 74(147), 82
Miller, S. L., 2(2), 23
Miller, W. W., 300(38), 305, 368(35),
370(35), 377
Milton, P. A., 91(41), 102
Mingioli, E. S., 7(48), 10(48), 24
Minor, P., 13(140), 27
Minot,G. R., 6(40, 41), 24
Minty 5 B., 346(186), 355
Mitchell, J. A., 13(140), 27
Miyazawa, E., 383(11), 415
Mm. Yurkevich, A., 161(52), 164
Mockel, W., 205(10), 230
Moe, P. G., 21(211), 22(211), 30
Molander,G.A.,156(21),163
Moldow,C,F.,339(108),352
Molin Christensen, J., 62(41), 65(41), 66
(41) , 67(41), 78
Moilin, D. L., 72(121), 73(126), 74(126),
81, 88(3), 92(3), 94(55), 95(69, 111),
97(69), 100,103, 104, 345(183), 355
Montejano, Y., 59(27), 78
Moore, E. C, 285(35), 289(73), 290(77,
IS), 415, 417
Moore, K. W., 238(17), 239(17, 22), 240
(17, 25), 243(17), 244(25), 259, 260
Moore, M. R., 175(86), 176(85, 86), 200
Moore, W. E. C, 170(40), 199
MoreU, A. G., 18(178), 29, 76(190), 84
Morelli, T. A., 70(56, 57), 75(56, 57), 79
Morgan, J. O., 97(61), 102
Morikawa, Y., 247(57, 62), 261
Morimoto, K., 256(93), 262
Morinaga, K., 383(11), 415
Morley, C G. D., 205(4), 207(4), 209(4),
210(4), 212(4), 213(4), 215(4), 218(4),
219(4), 220(4, 32), 222(32, 35), 223(35),
230(4), 230, 231
Morningstar, J. F., 339(97), 352
Morrow, G., 339(115), 352, 359(6), 376
Mortensen , E., 89(30), 101
Moschowitz, B., 20(191), 29, 73(132), 82
Moss, T. H., 269(26), 274(26, 40), 275(26),
276(26), 282(26), 286, 301(41,42), 305
Motokawa, Y., 194(142), 195(142), 202
Mottur, G. P., 35 (42), 42(42), 43(42), 44
(42) , 5 3
Mudd, S. H., 21(210, 211), 22(211), 30,
337(94), 339(114, 115, 119), 341(129),
342(137, 139), 352, 353
Muir, M., 72(102), 73(102), 81
Muller, G., 130(36), 139(36), 144(52), 148,
309(22), 349
Muller, O., 130(36), 139(36), 148, 309(22),
349
Munavalli, S., 385(51), 416
Munch-Peterson, A., 290(6), 297(26), 303,
304
Munck, O., 72(115, 116), 81
Murai, K., 5(28), 24, 248(65), 261
Murphy, W. P., 6(40), 24
Murray, B. K., 342(136), 353
Murray, R. M., 22(216, 217), 30
Murray-Lyon, I. M., 76(206), 84
Murthy, V. V., 363(24), 377
Musso, A. M., 95(69, 111), 97(69), 103,
104
Myasischeva, N. V., 158(33, 35), 161(52)
163,164
Myers, C, 7(53), 24
Myren, J., 71(64, 72, 73), 79, 80
NaegeU, H. U., 47(51), 54
Nakane, P. K., 71(63), 79
Nakatani, K., 339(106), 352
Nakazawa, T., 339(117), 342(117), 352
Nancekievill, D. G., 345(183), 355
Narahara 5 H., 5(28), 24, 248(65), 261
Nathan, H. A., 11(120), 27, 51(84), 55
Neal, G. E., 339(112), 340(112), 352
Neale, G., 20(195), 29, 75(164), 83
Neece, S. H., 174(73, 74, 75), 200
Neese, R. A., 239(21), 260
Neff, N. F., 389(73), 417
Neilands, J. B., 47(52), 54
Neimam, P. E., 73(123), 74(123), 81,98(98), 103
Netrawali, M. S., 50(73), 54
Neurauter, C, 169(27), 173(27), 175(27),
195(27), 198
Nevins, M. P., 34(10), 43(10), 52
Newman, G. E., 16(169), 28
Newmark, P. A., 89(31), 95(69, 111),
97(69),101,103,104
Nexo, E., 19(188), 20(188), 29, 58(12), 59
(24), 61(29, 38), 62(24, 29, 38,41, 211,
212, 214), 65(41), 66(12, 41, 43,45), 67
(41, 43, 45), 68(47), 69(12, 38,43, 50),
70(12, 38, 43, 50), 74(140, 146), 75(12,
140, 184, 187, 188), 76(12, 140, 184,
193), 77, 78, 79, 82, 83, 84, 85(222), 88
(8, 11), 89(8), 90(8, 110), 95(110,126),
96(123, 124), 98(11), 99(8), 100,104,
363(23), 377
N'Guyen Cong, H., 5(13), 23
Nichoalds, G. E., 45(50), 54
Nicolas, J.-P., 70(55), 71(82), 79, 80
Nieweg, H. O., 22(220), 30, 71(61, 86),
79, 80, 95(115), 104
Nisley, P., 257(97), 262
Nisonoff, A., 70(60), 79
Niswender, G. D., 95(116), 104
Nixon, P. F., 383(15), 384(15), 415
Norredam,K., 19(188), 20(188), 29, 75
(184), 76(184), 83
Norrell, S. A., 34(9), 45(9), 52
North, J. A., 339(116, 118), 340(118),
342(116,118,136), 352, 353
Northrop, D. B., 362(19), 364(19),
377
Nossal, N. G., 34(7), 52
Nunn, J. F., 346(186), 355
Nyberg, W., 98(88), 103
Nystrom, R. F., 368(34), 377
O'Brien, H. A. W., 72(121), 81
O'Brien, J. R. P., 16(169), 25
O'Brien, R., 71(95), 80
O'Brien, V. E., 175(86), 176(86), 200
O'Brien, W. E., 170(32), 172(32), 173
(62), 174(77), 175(32, 62, 77), 176(85),
178(32), 198,199, 200
Ochiai , E., 245(52),261
Ochoa, S., 17(171), 28, 358(1,4), 360(10,
11), 361(11), 364(10, 11, 26, 27), 365
(10), 366(10), 367(10), 371(27, 48),
372(27), 376, 3 77,378
0'Farell,P. H., 65(223), 85
Oginsky, E. L., 11(117), 26, 34(8), 52
Ogunfunmilade, Y. A., 98(77), 103
Ohashi, K., 37(19), 53, 236(16), 248(68),
259, 261
Ohmori, H., 339(101, 104,106), 352
Ohta, H., 7(54), 24
Ohwaki j K., 167(15), 198
Oikawa, T. G., 249(72), 261, 294(21), 304
Okada, K.., 144(51), 148
Olefsky j J. M., 74(157),
Olesen, H., 15(158, 163), 19(188), 20(163,
188), 29, 29, 58(5), 61(38), 62(38,41,
211, 214), 65(41, 222), 66(41, 43,45),
67(41, 43, 45), 68(47), 69(38,43, 50),
70(38,43, 50, 51), 73(168), 75(162,
168, 169, 184), 76(184), 77, 78, 79, 83,
84(210), 85, 90( 110), 95(60, 110), 96
(124), 97(60), 98(93), 102, 103,104
Olesen, H. A., 15(159), 28, 74(141), 82
O'Neill, B. J., 97(68), 103
Oppitz,K. H., 71(84), S0
Oren, R., 51(86), 55
Orgel, L. E., 2(2), 23
Orme-Johnson, W. H., 269(26), 274(26),
275(26), 276(26), 282(26), 286, 301
(42), 305, 406(107), 407(108, 109), 408
(108), 418
Orr, A. H., 76(206), 84
Orr, J. C, 274(38), 287
Orr, M. D., 385(46), 387(62, 63), 390(46),
392(46, 63), 394(62, 63), 397(63), 416
Ortiz, P. J., 358(1), 376
Osborne-White, W. S., 345(172, 174), 354
0stergaard Kristensen, H. P., 89(34), 98
(34), 101
Ostrowski, W., 4(11), 25
Ostroy, F., 74(150, 156), 82, 83
O'Sullivan, H., 347(190), 355
Overath, P., 301(39), 305, 358(5), 361(12),
363(12), 365(12), 366(12), 367(5, 12,
29), 368(12), 376, 377
Oxender, D. L., 45(50), 54
Ozaki, C, 256(93), 262
Paessens, A., 312(39), 350
Painter, K., 95(116), 104
Panagou, D., 387(62, 63), 392(63), 393
(83), 394(62, 63, 83), 397(63), 416, 417
Pannhorst, W., 374(66), 379
Pantskhava, E. S., 171(51, 52, 53, 54), 199
Paradinas, F. J., 76(206), 84
Parameswaran, K. N., 342(135), 353
Paranchych, W., 88(14), 101
Parker, D., 170(33), 171(33), 192(33), 196
(33), 198
Parker, D. J., 177(95), 179(108), 180(180),
201
Parker, D. V., 385(51), 416
Parker, J. L. W., 22(216, 217), 30
Parker, L. F. J., 16(164), 28, 37(20), 53
Parmentier, Y., 70(55), 71(82), 79, 80
Parsa,K.,345(171),554
Parsons, M., 73(137), 82
Pasher, I., 11(120), 27, 88(24), 97(24), 101
Pastan, I., 257(97), 262
Patchornik, A., 91(46), 102
Patel , L., 359(8), 376
Patel, N., 89(31), 707
Patmore, D. J., 152(5), 162
Pattison, J. R., 339(99), 352
Paukert, J. L., 176(79, 82), 200
Pawelkiewicz , J., 7(70), 10(109), 25, 26,
253(79, 80), 254(79, 80, 81, 82, 83), 257
(83), 262
Payne, W.J., 196(145), 202
Pchelkina, V. V., 171(51, 52, 53, 54), 199
Pearson, R. G., 154(14), 162
Pech , K., 254(82), 262
Peel, J. L., 317(51, 52), 350
Peirce j K., 74(149), 82
Penley, M. W., 152(8), 154(8), 162
Penrose j W. R., 45(50), 54
Perlman j D., 139(43, 44), 140(43,44,47),
141(47), 294(17), 148, 304
Perlman, K. L., 140(47), 141(47), 148
Perlman, R. L., 257(97), 262
Perry, J., 345(175, 176), 346(186, 188),
354, 355
Peterkofsky, A., 309(18), 310(18), 320
(18), 329(18), 339(18), 340(18), 349
Peters, C L., 345(165), 354
Peters, T. J., 72(100), 80, 99(105),
104
Petersen, R. A., 51(84), 55
Peterson, D., 389(73), 417
Peterson, W. H., 168(21), 169(21), 198
Petrocellis, B. C, 389(71), 417
Peytremann, R., 17(172), 28
Pfau, A. A., 71(84),
Pfeffer, R. D., 89(33), 101
Pfiffner, J. J., 107(10), 108(12, 13, 15),
117(10), 119(10), 120(10, 12), 121(10,
12, 13), 126(10, 12), 128(10, 12, 15,
34), 129(15, 34), 130(34), 131(15), 133
(34), 135(15, 34), 139(12, 34), 147,148
Phares, E. F., 368(32), 377
Picket, W., 151(4), 152(4), 162
Pine, L., 170(43), 171(43), 199
Pinter, I. J., 8(76), 10(103), 25, 26
Piperno, J. R., 45(50), 54
Pirrie,T. G., 22(215), 30
Plastow, G. S., 35(45), 43(45), 54
Plaut, G. W. E., 5(16), 23
Pluss, H. J., 73(125), 74(125), 81
Podell, E., 7(61), 12(61), 17(61), 25, 71
(81), 80, 88(25), 95(25), 96(119), 97
(25), 101,104
Podell, E. R., 18(176), 29, 71(87), 80,
96(118), 104
Porges, N., 6(35), 24
Porter, J. W. G., 12(125), 27
Pospelova, T. A., 91(40), 102
Poston, J. M., 3(9), 23, 173(58), 177
(99, 100, 101), 178(99, 100,101), 180
(100), 181(100), 184(58), 199, 201,
205(7), 227(7), 228(7, 44, 45, 46,47),
229(7, 44,47), 230(7), 231, 232
Powell, D. E. B., 93(51), 102
Poznanskaja, A. A., 235(11), 236(11),
237(11), 238(11), 259
Poznanskaya, A. A., 254(86, 87), 257(87),
262
Pratt, J . M ., 61(30), 78, 90(35), 91(35),
92(35), 101, 152(8), 154(8), 155(16),
156(16), 162, 1 63, 315(45), 346(184),
350, 355
Preston, Y. A., 35(11), 36(11), 37(11), 40
(11), 52
Pricer, W. E., 192(127), 202
Pringsheim, E. G., 50(78), 55
Prins, R. A., 167(17), 198
Provasoli, L., 7(51), 8(76, 77), 10(103)
24, 25, 26
Puutula, L., 59(21), 78, 97(64), 102
Quadros, E. V., 158(33), 163
Quastel, J. H., 257(95, 96), 262
Quayle, J. R., 194(137), 202
Queen, M., 191(123), 202
Rabinowitz, J. C, 170(38), 173(56), 176
(79, 82), 192(127, 129, 130), 195(144)
199, 200, 202
Rachele, J. R., 308(2), 342(2), 348
Rachmilewitz, B., 20(191, 194), 29, 73
(132, 135), 75(165, 173, 186), 76(200,
202), 82, 83, 84, 99(100), 104
Rachmilewitz, M., 20(191, 194), 29, 73
(132, 135), 75(165,186), 76(200, 202),
82, 83, 84
Radom, L., 376(72), 379
Rahat, M., 10(110), 26
Raibaud, P., 5(13), 23
Rakow, S., 153(13), 162
Randies, C H., 234(4), 256(4), 259
Ranlbv, P., 71(98), 80
Rao, S. S., 6(37), 24
Rapp, P., 93(106), 104, 145(59), 148,
247(59, 61), 261
Rappazzo, M. E., 15(156), 28, 73(133),
82
Rauch, B., 44(48), 54
Rauschenbakh, M. O., 161(52), 164
Raven, J. L., 88(6, 22), 90(6), 91(6, 22),
92(6), 97(6, 22, 61, 65, 76), 98(90),
100,101,102,103
Read, A. E., 98(78), 103
Redfield, B. G., 309(18), 310(18, 31),
313(41), 320(18, 31), 329(18), 339(18,
107, 111), 340(18, 111), 341(111),
349, 350, 352
Redmond, J. W., 372(58), 378
Reed, B., 346(187), 347(190), 355
Reeder, D. J., 174(70), 200
Rees,G. M., 345(183), 355
Reeves, R. B., 51(83), 55
Reeves, R. E., 257(100), 262
Regelson,W.,75(170),^J
Reich, K., 10(110), 26
Reichard, P., 383(32), 385(35, 38,48),
386(48), 389(48, 69), 390(77, 78),
393(48), 413(122, 123), 415, 416,
417, 418
Reimer, M., 152(5), 162
Reiquam, C W., 76(207), 84
Reizenstein, P., 75(182), 83
Reizenstein, P. G., 71(67), 79
Renz, P., 7(67), 25, 192(126), 202, 205
(2), 207(2, 14), 209(2), 210(2), 211(2),
212(2), 213(2), 218(2), 219(2), 230(2),
230, 231
Retey, J., 222(36, 37), 231, 242(36), 243
(39), 260, 268(22), 269(27, 28), 270
(27) , 272(27), 278(49), 281(27), 283
(28) , 286, 287, 362(16), 363(16), 364
(16) , 365(16), 366(16, 28), 367(16),
368(28), 369(28, 36, 37, 38), 370(42),
371(45, 47, 50), 372(51, 52, 53, 56, 57,
58, 61), 373(37, 63), 374(36, 62, 64,
66), 377, 378, 379
Retief, F. P., 73(131), 52
Reuwer, J. F., 282(55), 287, 369(38), 378
Reynolds, E. H., 345(176), 355
Reynolds, P. R., 35(42), 42(42), 43(42), 44
(42), 5 3
Ribbons, D. W., 194(136), 202
Richards, J. H., 238(17), 239(17, 20,
22), 240(17, 25), 243(17, 20), 244(25),
259, 260, 300(37, 38), 505, 368(35),
370(35), 377
Rickes, E. L., 16(165), 28
Riddle, M. C, 22(213), 30
Ridley 5 W. P., 152(11, 12), 153(13), 155
(17) , 156(17), 157(27), 161(12, 17),
162,163
Ridsdale, S. C, 152(8), 154(8), 155
(16), 156(16), 162,163
Riepertinger, C, 364(25), 377
Rietz, P., 37(21), 53
Rimerman, E. A., 207(16), 231
Ripley, D., 97(67), 98(81), 102, 103
Ritari, S. J., 317(59), 350
Ritter, G. J., 168(21), 169(21), 198
Robbins, W. J., 8(71), 25
Robertson, J., 71(94), 80
Robertson, J. A., 71(96), 80
Robins, E., 391(81), 417
Robinson, J. R., 194(139), 202
Robinson, W. G., 404(102), 418
Robson, M. B., 88(6, 22), 90(6), 91(6, 22),
92(6), 97(6, 22, 61, 65), 98(90), 100,
101, 102, 103
Roche, T. S., 158(38), 163
R0dbro, P., 71(65), 79
Rodriguez, E., 51(84), 55
Rooze, V., 230(53), 232, 291(10), 292
(16), 293(10), 295(10), 298(16), 304
Rosales, F., 317(59), 350
Rose, W. C, 340(126), 353
Roseman, S., 44(48), 54
Rosen, C G., 152(6), 162
Rosen, H., 229(48), 232
Rosenberg, L. E., 74(148, 154, 155), 82,
83, 88(13), 99(102), 100, 104, 340
(123), 341(130, 131), 342(139), 344
(152), 353,354, 359(7, 8), 376
Rosenblatt, D. S., 343(143a), 353
Rosenblum, C, 7(62, 69), 12(129), 25,
27
Rosenthal, H. L., 12(128), 13(142), 27
Rosenthal, S., 309(11, 12, 17, 27), 317
(17, 53, 54), 318(12), 319(27), 320(27),
322(54), 327(27), 328(17, 54), 329(17,
27), 336(27), 339(53), 340(54), 349,
350
Ross,G. I. M., 88(2), 100
Ross, P. D., 337(94), 352
Rossi, M., 389(71), 417
Roth, J., 74(158), 83
Rothenberg, S. P., 7(60), 25, 61(32), 71
(83), 72(101, 104, 105), 73(101), 78, 80,
81, 91(44), 95(109), 102,104
Rother, M., 344(157), 354
Rowe, P. B., 343(145), 347(189), 353,
355
Rowley, G. R., 74(147), 82
Ruben, S., 168(23), 170(23), 198
Rubin, E. M., 410(117), 411(117),
418
Rubin, M., 6(44), 24
Rubin, R., 73(144), 74(144), 82, 98(94),
103
Rubinson, V. A., 128(31), 148
Rudakova, I. P., 91(40),/02
Rudakova, J. P., 158(32), 161(52), 163,
164
Ruddle, F. H., 344(152), 354
Rudiger, H., 309(26), 310(37), 311(37),
312(39), 317(37, 55), 318(64), 328
(82), 336(89), 337(82), 338(55, 82),
349, 350, 351
Ruediger 5 H., 160(43,44), 164
Rush, J. E., 315(47), 350
Rusk-Madsen, J., 71(98), 80
Russell, S. A., 384(17), 386(17), 391
(17), 415
Rutberg, L., 389(69), 417
Ryback, G., 372(51), 378
Rye, M., 84
Ryel,E. M., 74(156), 83
Saarni,M.,98(88), 103
Sabet,S. F., 42(39), 53
Sachs, M. V., 71(85), 80
Sadasivan, N., 128(33), 131(33), 148
Sagers, R. D., 192(128), 194(132, 133,
138, 139, 140, 143), 202
Sagerson, R. N., 73(124), 74(124), 81
Sahashi, Y., 383(11), 475
Saiki,T., 174(65a),200
Sakami, W., 309(13), 317(59),
339(13), 349, 350
Salem, A. R., 194(137), 202
Salem, L., 376(73), 379
Salem, M. E., 347(189), 355
Salonen, E. -M., 58(8), 61(35), 71(77),
73(136), 77, 78, 80, 82, 96(120), 104
Salter, W. T., 6(41), 24
Sanders, E.G., 61(36), 78
Sanders, M., 51(84), 55
Sando,G. N., 11(113), 26, 384(21),
386(21), 388(21), 390(21), 392(21),
393(21), 398(21), 399(21), 400(21,
91, 92), 401(91, 92), 404(21), 406(91),
409(56, 91) , 412 (56, 91) , 415, 4 16, 417
Sands, R. H., 245(51), 261, 275(42),
287, 409(112), 418
Sanfilippo, A., 5(21), 23
Sansom, B. F., 12(132), 27
Sasakawa, T., 364(26, 27), 371(27, 48),
372(27), 377, 378
Sasaki, K., 106(6, 7), 109(6, 7), 147
Sasaki, T., 49(64, 65, 66, 67, 68),
54
Sastry, C A., 6(37), 24
Sato, K., 6(32), 9(93), 24, 26, 59(26),
78, 107(9), 109(9), 147, 240(27),
244(27), 260, 274(38), 287, 310(32),
311(32), 320(32), 339(101, 103),
349, 352
Sato, S., 70(60), 79
Sauer, H., 343(144), 345(166), 353, 354
Sauer, H. -J., 17(173), 28
Savage, C. R., 64(217), 70(57), 73(130,
134), 75(57), 79, 82, 85
Saveant, J. M., 160(41), 164, 337(92),351
Scarlett, F. A., 33(2), 52, 264(5, 6),
265(5), 286
Schaad, L., 369(38), 378
Schaad, L. J., 282(55), 287
Schachman, H. K., 398(88), 408(88), 417
Schacht, J., 205(10), 230
Schafer, D. E., 71(78), 80
Schaller, K., 41(37), 53
Schaupp, A., 169(27), 173(27, 63),
175(27), 195(27), 198, 199
Scheffel, U., 88(23), 95(23), 97(23),
101
Schepler, K. L., 245(51), 261, 275(42),
287, 409(112), 418
Scherer,P. A., 174(67), 200
Scherrer, R., 49(59), 54
Schilling, R. F., 95(56), 102
Schjonsby,H.,71(8O),S0
Schlegel, H. G., 167(9), 168(9), 169(9),
170(9), 198
Schlesinger, M., 20(194), 29, 73(135), 82
Schlingmann, G., 106(4, 8), 109(4, 8, 16)
110(4, 8), 111(4), 112(4), 114(4), 115
(8, 25), 117(4), 121(4, 8, 16), 122(4,
8, 27, 28, 29), 123(4, 8, 16, 25, 30),
125(8, 16, 25), 126(16), 131(38), 135
(4), 138(4), 145(4, 8, 16), 147,148
Schlossmann, K., 362(18), 377
Schmitt, T., 181(111, 112), 201, 205(11), 230
Schmidt, U., 161(50, 51), 164
Schobert, S., 166(6), 167(6), 168(6),
196(6), 198
Schoberth, S., 168(19, 20), 198
Schomer, U., 140(47), 141(47), 148
Schnaitman, C. A., 39(29), 40(34),
41(35), 42(34), 43(35, 46), 53, 54
Schneider, P., 112(22), 117(22), 131(22),
147
Schneider, R. J., 15(160), 28, 74(142),
76(189), 82, 84
Schneider, Z., 253(80), 254(80, 82, 83, 84,
85), 257(83), 262
Schrauzer,G. N., 133(39), 148, 155(20),
160(20), 163, 179(107), 108(107), 201,
245(53, 54, 55), 246(53, 54, 55), 261,
278(43, 44, 45), 287, 338(96), 352,
410(115, 116, 117),411(117, 118), 418
Schrecker, A. W., 389(70), 417
Schreiber, C, 20(202), 30
Schrich, L., 176(81), 200
Schrumpf, E., 71(72, 73), 79, 80
Schulman, J. D., 21(210), 30, 339(119), 352
Schulman, M., 170(33), 171(33), 176(92),
177(92), 178(106), 179(106), 182(92),
189(106), 192(33), 196(33), 198, 201
Schultz, R. M., 279(50), 287
Schulze,P., 248(67), 261
Schwartz, M., 15(163), 19(188), 20(163,
188), 21(208), 28, 29, 30, 70(51),
73(168), 75(168, 184), 76(184), 79,
83, 98(93), 103
Schwartz, S., 7(64), 25, 71(64), 79
Schweigert, B.S.,415
Scott, A. I., 144(51, 54), 145(56, 57),
148, 1 49, 374(68), 379
Scott, H. W., 11 (111), 26
Scott, J., 89(33), 101
Scott, J. M., 15(154), 28, 318(67), 345(168,
169), 346(187), 347(190), 351, 354, 355
Scott, K. J., 12(132), 27
Scott, R., 73(124), 74(124), 81
Scovell, W. H., 155(15), 163
Scrimgeour, K. G., 309(16), 320(71), 339
(16,11), 349, 351
Seek, J. A., 278(44), 287, 410(115, 117),
44(47), 418
Seelers, T. D., 155(18), 156(18), 163
Seetharam,B., 18(176), 29, 71(81, 87), 80,
96(118,119), 104
Segal, G., 376(73), 379
Seibl, J., 242(36), 260, 278(44), 287, 372
(51), 378
Seidel,S.L., 161(47), 164
Sekizawa, Y., 291(9), J04
Selhub, J., 75(173), 83, 99(100), 104
Seligman, P. A., 63(39), 64(39), 74(39),
78
Serfilippi, D., 71(62), 74(143), 79, 82
Sgherzi, A. M., 88(5), 700
Shackleford, G., 174(65a), 200
Shafer,R.B.,97(67),702
Shane, B., 342(132), 353
Shannon, R., 40(33), 53
Shapiro, M., 374(65), 379
Shaw, N., 130(37), 148, 309(21), 349
Shaw, W., 97(75), 103
Sheldrick, W. S., 122(26, 27), 123(30),
131(26, 38), 147, 148
Shemin,D.,7(62,63), 11(123), 25, 27
Shia, M. A., 74(151), 82
Shin, J., 209(24), 226(24), 231
Shilling, R. F., 385(33), 415
Shimizu,S.,6(32),9(93),2¥, 26, 59(26),
78, 107(9), 109(9), 147, 219(31), 231,
239(19), 241(30, 31), 242(31), 243
(19), 246(30, 31), 247(57,62), 248
(63), 251(74), 260, 261, 262, 310(32),
311(32), 320(32), 339(101, 102, 103,
106), 349, 352
Shin, Y. S., 345(167, 170), 354
Shinton, N. K., 20(206), 30, 98(79), 103
Shirakashi, T., 23(7), 238(7), 239(7), 240
(7), 247(58), 259, 261
Shoaf, W. T., 174(75), 200
Shorb, M. S., 6(45, 46), 24, 88(1), 700
Shum,H. -Y., 97(68), 103
Sibert, J. W., 179(107), 180(107), 207
245(53), 246(53), 261, 278(43), 287,
410(117), 411(117, 118), 418
Siddons, R.C., 12(126), 27
Silber, R., 339(108), 352
Silverman, R. B., 280(53), 281(53), 287
Silvis,S.E.,98(81),70J
Simnett, K. I., 12(134), 27
Simon, H., 373(62), 378
Simons, K., 20(192), 29, 59(18, 19),
75(181), 78, 83
Simpson, G. G., 2(4, 5), 3(5), 23
Singh, D., 387(65), 392(65), 394(65),
395(65), 396(65), 397(65), 398(65),
405(65), 408(65), 416
Sinkkonen,I.,59(18, 19), 78
Sjoberg, B. M., 383(31), 413(123), 415
Skarzynski, B., 4(11), 23
Skeggs, H. R., 382(2), 386(2), 414
Skoog, F., 10(101), 26
Slaby,I., 385(44), 416
Sladden, R. A., 73(126), 74(126), 81
Smiley, K. L., 253(78), 256(94), 262
Smith, C. M., 5(16), 23
Smith 5 D. A., 322(75, 76), 351
Smith, E. H., 369(37), 373(37), 378
Smith, E. L., 5(27), 6(39), 9(94), 16(164),
24, 26, 28, 37(20), 53, 130(37), 148,
309(20, 21), 349
Smith, E. W., 371(45), 378
Smith, G. W., 61(36), 78
Smith, J., 12(133), 27
Smith, L. C, 309(27), 317(54), 319(27),
320(27), 322(54), 327(27), 328(54),
329(27), 336(27), 340(54), 349, 350
Smith, M. R., 166(5), 198
Smith, P. H., 166(3), 797
Smith, R. A., 158(34), 163, 310(30), 342
(140), 343(147), 347(147), 349, 353
Smith, R. M., 345(172, 174), 354
Smith, S. G., 152(8), 154(8), 762
Smith, T. A., 7(53), 24, 249(73), 261
Smyth, R. D., 230(51), 232, 290(3,4,
5, 6), 29(4, 15), 299(36), 303, 304,
305, 358(3), 376
Snell, E. E., 10(107), 26, 382(1, 3, 4),
383(4), 386(1, 3, 4), 414, 415
Snell, N. S., 11(115), 26
Sobolov, M., 253(78), 256(94), 262
Sobotka,H., 11(120), 27, 88(24),
97(24), 707
Soda, K., 235(11), 236(11), 237(11),
238(11), 259
Soderberg, B. -O., 385(39, 43, 45), 416
Soderhall 5 S., 385(37), 416
Soderhjelm, L., 98(83), 103
Sofina, Z.P., 161(52), 164
Sols, A., 257(100), 262
Somack, R., 225(43), 226(43), 231
Sonneborn, D. W., 75(170), 83
Sourial, N. A., 73(126), 74(126), 81,
94(55), 102
Southcott, B. A., 9(98), 26
Spande,T.F.,91(46),702
Spears, C, 322(77), 342(138), 351, 353
Spell, W.H., Jr., 383(7), 415
Spencer, T. E., 174(74), 200
Spies, T. D., 22(219), 30
Spray, G. H., 12(134), 16(169), 20(207),
27, 28, 30, 93(48), 95(71), 97(71), 98
(92) , 7 02, 103
Sprecher, M., 297(28), 298(29), 300
(29), 301(29), 304, 371(49), 372(49,
55), 378
Sprinson, D. B., 7(69), 25, 297(28, 29) ,
300(29), 301(29 ), 304, 371(49), 372
(49, 55), 378
Spronk, A. M., 345(181), 355
Spudich,E.N., 47(54), 54
Sreenivasan, A., 50(73), 54
Stadlbauer, E. A., 278(45), 287
Stadtman, E. R., 167(16), 173(58), 177
(99, 100, 101), 178(99, 100, 101, 105),
180(100), 184(58), 198, 199, 201,
211(26), 230(26), 231, 264(3), 265(3,
11), 266(3, 11), 267(3), 268(3), 286,
301(39),305, 358(5), 361(12), 363(12),
365(12), 366(12), 367(5,12, 29), 368
(12) , 376,377
Stadtman, T. C, 3(9), 23, 171(48, 49, 50),
199, 205(1, 2, 3, 4), 206(13), 207(1, 2, 3,
4, 13,14, 18, 19), 208(13, 19), 209(2, 3,
4, 19, 21, 22, 23, 24), 210(2, 4, 13, 19,
25), 211(2, 19), 212(1, 2, 4, 19), 213
(2, 3, 4, 19), 214(19), 215(4, 19), 216
(13) , 217(19), 218(2, 4, 13, 19, 25),
219(1, 2, 4, 13,19), 220(4, 19, 32), 221
(34), 222(32, 35, 36, 37), 223(13, 19, 35,
39), 224(21), 225(19), 226(1, 3, 23, 24),
230(1, 2, 3, 4, 21, 22, 54), 230, 231, 232,
264(1), 286, 296(23), 299(23), 304, 372
(56), 378
Stafford, W. H., 37(20), 53
Stahlberg, K. -G., 7(55), 16(55), 19(187),
24, 29, 88(18), 101, 344(161), 354
Stamm,D.,89(28),i07
Starr, T. J., 8(74, 75), 25
Stavrianopoulos, J., 310(33), 311(33),
314(33), 317(33), 318(33), 320(33),
328(33), 336(33), 350
Stebbins,M. E., 8(71), 25
Stebbins, R., 15(154), 28
Steen, V. D., 359(1), 376
Steinberg, W. M., 71(79), 80
Stenman, U. -H., 15(152), 20(192), 28,
29, 58(11), 59(20, 23), 61(33), 65
(42), 73(136), 77, 78, 82, 88(91),
97(64), 100, 102
Stephenson, M., 257(95, 96), 262
Steuart, B. W., 339(118), 340(118), 342
(118), 352
Stevenson, I. L., 11(112), 26
Stivers, E. C, 282(55), 287, 369(38),
378
Stjernholm, R., 297(25), 304, 359(9),
361(13), 362 (17), 363(13) , 365 (13),
366(13), 367(13), 377
Stock, J. B., 44(48), 54
Stokstad, E. L. R., 7(51), 24, 339(113),
340(120), 342(132), 344(158, 159),
345(158, 159, 167,170), 352, 353, 354
Stopa, E., 71(95), 80
Stopa, E. G., 71(93), 80
Strayer,R.F., 166(4), 197
Streeter, A.M., 97(68), 103
Strength, D. R., 16(168), 28
Strickland, J. D. M., 8(83), 25
Stroinski, A., 253(81), 254(81, 84),
262
Strubbe, J., 412(121), 418
Stryer, L., 385(38), 416
Stutzenberger, F., 384(22), 386(22), 390
(76), 393(22), 415, 419
Suckling, C J., 268(22), 286, 372
(57), 378
Sugimoto, Y., 219(31), 231, 241(30, 31),
242(31), 246(30, 31), 260
Suhadolnik, R. J., 403(97),
Sultan, C. 20(193), 29, 76(201, 208),
Sund, H., 362(16), 363(16), 364(16), 365
(16), 366(16), 367(16), 377
Sutton, T. S., 5(12), 23
Suzuki, F., 230(53), 232, 291(10, 12),
293(10, 12), 295(10), 296(12), 298
(12, 16),304
Suzuki, T., 383(11), 415
Swain, C G., 282(55), 287, 369(38), 378
Swallow, A. J., 346(185), 355
Swan, H. T., 20(207), 30
Swenson, C. A., 315(47), 350
Swett, V. C, 141(49), 148, 344(156),
354
Swick,R.W., 368(30), 377
Swim, H. E., 184(121b), 202
Swingle, S. M., 363(21), 377
Switzer, R. L., 291(13), 292(13),
293(13), 294(13, 20), 295(13), 296
(13, 20), 297(28), 299(20), 300(13,
20), 304, 372(55), 378
Tachkova, E. M., 158(35), 163
Takasugi, M., 339(117), 342(117), 352
Takeuchi, H., 339(102), 352
Takeyama, S., 308(5), 311(42), 314(42),
318(63), 337(42), 342(42), 349, 350, 351
Talas, A., 112(18), 117(18), 747
Tamao, Y ., 21 9(31), 231, 241(30, 31) ,
242(31), 246(30, 31), 247 (57, 6 2), 260,
261, 387(65), 392(65), 3 94(65), 395
(65), 396 (65), 397(65, 87
), 398(65),
400(90), 40 6(90, 106), 408(65
, 90),
10(106), 412(9
0),
416,
409(87), 4
417,418
Tamikubo,T., 106(6), 109(6), 147
Tan, C H., 70(59), 79
Tan, L. U. L., 176(80), 200
Tanizawa, K., 235(11), 236(11), 237(11),
238(11), 259
Tanner, R. S., 166(6), 167(6), 168(6, 18),
172(18), 175(18), 178(18), 196(6), 198
Tarr,H.L. A., 9(98), 26
Tatsis, B., 70(52), 73(52), 75(52), 79
Tavill, A. S., 73(129), 52
Tave, J. L., 49(61), 54
Taylor, P. J., 12(132), 27
Taylor, R., 211(27), 231, 314(43), 350
Taylor, R. T., 34(9, 10), 43(10), 45(9),
52, 91(37), 101, 157(26, 29), 160(42),
163, 164, 176(88, 89), 177(93), 182
(114), 186(93), 200, 201, 309(25),
310(28, 29, 35, 36), 311(28), 312(28,
35), 313(35, 36), 314(28, 35), 315(46),
316(48), 317(28, 46, 48,49, 50, 56, 57),
318(62, 68), 319(28, 69), 320(28, 29,
46, 49, 56, 70, 73), 321(28, 56, 62),
322(29, 35, 46, 56, 69, 70, 78), 325(29,
79), 326(69, 80, 81), 328(50, 80, 81),
329(50, 84, 85), 330(56, 70), 331(56),
333(56, 62, 86), 336(28,49, 56), 337
(28, 46, 49, 62, 70, 85), 338(25, 50),
341(25), 342(28, 142), 343(142), 345
(163,178, 179,180), 349, 350, 351, 353,
354, 355
Tejerina,G., 11(122), 27, 33(3), 52, 308
(9, 10), 349
Teng, C. C, 73(124), 74(124), 81
Thauer, R. K., 2(6), 23, 32(1), 52, 173
(59), 174(67, 71), 186(120, 121), 199,
200, 201
Thelander, L., 383(31), 390(78), 410(114),
415, 417,418
Thenen, S, W., 344(158), 345(158), 354
Thexton, R. H., 9(88), 11(88), 26
Thomas, J. H., 93(51), 102
Thomsen, J., 62(41, 211, 212, 214), 65
(41), 66(41, 43, 45), 67(41, 43, 45),
69(43), 70(43), 78, 54(210),55(222),
90(110), 95(110), 104
Thomson, A. J., 115(24), 131(24), 147
Thorndike, J., 17(172), 28
Thornton, J., 157(30), 163
Tibbling, G., 97(74), 103
Tiedje, J. M., 166(4), 197
Tietz, N. W., 89(29), 101
Tipper, D. J., 48(58), 54
Tiselius, A., 363(21), 377
Tkachuck, R. D., 37(22), 53, 313(40),
350
Tobimatsu, T., 240(24), 244(24), 260
Todd, A. R., 37(20), 53
Toler, L. A., 345(165), 354
Toohey, J. I., 6(30, 31), 24, 106(1, 5) ,
107(5), 108(1, 5), 10 9(5), 110( 113),
114(1,5), 117(1,5), 139(1,43,44),
140(43,44), 146,147,148, 230(52),
232, 290(6), 29 4(17), 299(36), 303,
304, 305
Tookey, J. I., 5(22), 25
Topich, J. A., 158(38), 163
Toraya, T., 37(19), 53, 219(31), 231, 235
(7, 8, 9, 11), 236(11, 13,14, 15,16),
237(11, 14, 15), 238(7,11), 239(7),
240(7, 24), 241(13, 28, 29, 30, 31),
242(13, 14, 15, 28, 31), 244(24, 89),
245(9), 246(13, 28, 30, 31), 247(9,
15, 58, 60), 248(9, 60, 68, 69, 73),
249(8, 70, 71), 251(7, 8, 75), 252
(76), 253(76), 254(88, 89), 255(89,
91), 256(89, 92), 257(88, 89, 91, 101),
258(101, 102), 259, 260, 261, 262,
296(24), 304
Tortolani j G., 99(104), 104
Toskes, P. P., 61(36), 71(79), 78, 80
Townsend,C. A., 144(51), 145(56), 148,
149
Townsend, L. B., 402(96), 403(96), 417
Townsend, W. C, 58(15), 78
Trachtenberg, A., 72(119), 81
Trager, L., 383(8), 475
Trebst, A., 7(65), 25
Trier, J. S., 72(114), 73(114), 81
Tripp, E., 76(196), 84, 343(145), 345
(171, 173, \11),353,354, 355
Tsai, L., 205(1, 3), 207(1, 3), 209(3), 212
(1), 213(3), 219(1), 226(1, 3), 230(1, 3,
5A), 230, 232
Tsai, P. K., 384(26), 386(26), 388(26), 393
(26), 398(26), 399(26), 404(26), 405(26),
415
Tsuda, Y., 205(6), 223(6), 225(6), 230
(6), 230
Tu,S.-T., 70(60), 79
Tudhope, G. R., 20(207), 30
Tung, A. S., 70(60), 79
Turano,C, 220(33), 231
Turner, A.M., 157(30), 163
Turner, J. M., 33(2), 52, 264(5, 6, 9), 265
(5,9, 13), 266(9), 268(9), 286
Uchida, Y., 248(66), 261, 294(19), 304
Ueno, H., 248(68), 261
Uesaka, M.„ 236(14, 15), 242(14, 15),
247(15), 259, 296(24), 304
Uhlendorf, B. W., 21(211), 22(211), 30, 342
(137, 139), 353
Ukstins, I., 309(13), 339(13), 349
Umani-Ronchi, A., 242(36), 243(39), 260,
269(28), 278(49), 283(28), 286, 287, 372
(53), 373(63), 378
Ungley, C.C., 12(124), 27
Ushio, K., 235(8), 244(8), 248(8), 249(8,
71), 251(8), 258(102), 259, 261, 262
Uyeda, K., 192(129, 130), 202
Vahlquist,B.,98(84),7
Valencia,R.,5(13),
Valinsky, J., 240(27), 244(27), 245(47),
260, 261, 301(43), 305
Valinsky, J. E., 242(37), 245(48, 49), 260,
261, 305(44), 305
van Baalen,C, 10(102), 26
van D er D rift, C, 192(131) , 19 5(131), 202,
208(19), 20 9(19), 210(19), 211(
19), 212
(19, 28) , 213 (19), 214(1 9), 2 15(19), 217
(19), 21 8(19, 30 ), 219(1 9), 2 20(19), 223
(19), 225(19), 231
Vanderplas, L., 73(131), 52
van Der Weyden, M. B., 344(157, 160), 354
van De Wiel, D. F., 95(115), 104
van Dommelen, C K. V., 22(212), 30
van Kapel, J., 62(213), £4
van Leeuwenhoek, A., 166(2), 197
Varma, T.N. S., 50(76), 55
Vatn, M. H., 71(68, 72, 73), 79, 80
Veeger,C, 372(51), 378
Veeger,W.,71(86),50
Veillard, A., 376(73), 379
Venkataraman, S., 50(73),54
Veno, H., 37(19), 53
Vetter,H., Jr., 205(10), 2J0
Victor, M., 19(181), 29
Vidal, A. J., 344(159), 354
Vilter,C. F., 22(219), 30
Vilter, R. W., 22(219), 30
Vischer, D., 73(125), 74(125), 81
Visser, H., 73(131), 52
Visuri, K., 59(20, 22), 78
Vitins,P., 75(179), 83
Vitols, E., 383(15), 384(15), 385(46, 47,
49), 386(47, 49), 387(49), 390(46, 49),
392(46, 49), 493(49), 394(49, 85), 395
(49), 396(49), 397(49), 399(49), 400
(49), 404(104), 405(104), 410(85),
415, 416,4ll(19) i 418
Vitols, K . S ., 3 17(61), 33 4(61), 337(61),
338(61), 343(61), 350
Vogelmann, H., 37(21),
53, 99(103), 104,
108(14), 145(59), 147, 148
Vogels, C D., 166(2), 192(131), 195
(131), 797, 202
Voisenet, C E., 234(3), 259
Volcani, B.E., 5(22),2J, 167(14), 171(47),
198, 199, 290(6), 299(36), 303, 305
von Bonsdorff, B., 98(88), 103
von der Lippe, G., 71(80), 80
Waber, L.
J., 1 70(39), 171 (39), 192(39),
193(39), 195(39), 196(39), 799
Wachsman, J. T ., 2 30(50), 232, 290(2),
303, 384(20), 386(20), 38 9(20), 393
(20), 415
Wachters, J. J., 71(61), 79
Wack,J.P., 16(168), 28
Wacker, A., 333(8), 415
Wagle, A., 94(54), 102
Wagner, F., 37(21), 53, 99(103), 104, 108
(11, 14, 15), 128(15, 34), 129(15, 34,
46), 130(34), 131(15), 133(34), 135(15,
34), 139(34), 143(50), 145(59), 147, 148
Wagner, H . N., 88(23), 93(50) , 9 5(23), 97
(23), 101, 102
Wagner, O. W., 240(26), 244(26), 260,
272(34), 287
Wagner , R., 174(69), 200
Wagstaff, M., 97(66), 102
Walker, P. L., 88(6), 90(6), 91(6), 92(6),
97(6, 76), 98(90), 100, 103
Walker, T. E., 37(24), 53, 247(62a), 261
Wallace, J. K., 74(151), 82
Wallach f R. C., 156(23), 163
Walling, C, 376(70), 379
Wallis, 0. C, 265(10), 266(14), 269
(25), 274(25), 275(25), 276(25), 283
(25), 286, 371(45), 378
Walsh, C, 412(120),418
Wang, F. K., 340(120), 352
Wang, L., 73(137), 82
Warmuth, E., 106(4), 108(4), 109(4), 110
(4), 111(4, 17), 112(4, 17), 114(4), 117
(4, 17), 118(4), 121(4), 122(4), 123(4),
135(4, 17 ), 13 8(4), 145(4 , 17) , 147, 14 8
Warner, R. C, 360(10), 364(10), 365(10),
366(10), 367(10), 377
Wasserman, L. R., 7(59), 25, 97(73), 103
Waszinski, H. M., 194(136), 202
Waters, W. E., 98(82), 103
Watson, C J., 7(64), 25
Wawszkiewicz, E. J., 290(4), 291(4), 303
Waxman, S., 20(200, 202), 29, 30, 64(219),
75(183), 76(183), 83, 85, 141(49), 148,
344(156), 354
Weber, J. H., 133(39), 148
Weber, T., 75(181), 83
Wehnert, M., 339(105), 352
Weinreb,N., 20(198), 29, 75(163), 83
Weir, D. G., 318(67), 346(187), 347(190),
351, 355
Weisblat, D. A., 267(19), 269(19), 272(19),
278(19), 281(19), 286
Weiss, J. B., 50(75), 55
Weiss, J. P., 61(32), 71(83), 72(101, 105),
78, 80, 81
Weiss, M. J., 39(26), 53
Weissbach, H., 176(88), 177(93), 182(113,
114), 186(93), 200, 201, 211(27), 230
(51, 52), 231, 232, 290(5, 6), 291(15),
299(36), 303, 304, 305, 309(18, 25), 310
(18, 28, 31), 311(28), 312(28), 313(41),
314(28, 43), 315(46), 317(28, 46, 49,
50, 56, 58), 318(68), 319(28), 320(18,
28, 31, 46, 49, 56, 70, 73), 321(28,
56), 322(46, 56, 70, 74, 77), 326(28,
50, 80, 81), 328(50, 80, 81), 329(18,
50, 84, 85), 330(56, 70), 331(56),
333(56), 336(49, 56), 337(25, 28, 46,
49, 70, 85), 338(25, 50), 339(18, 107,
111), 340(18, 111), 341(25, 111), 342
(28, 38), 344(150), 349, 350, 351, 352,
358(3), 376
Weitz, M. A., 72(118), 81
Welty, F. K., 176(90), 182(90), 184(90),
190(90),201, 338(95),352
Werkman, C H., 234(2), 259
Weygand, F., 7(65), 25
Weyhenmeyer, R., 192(126), 202
Whetham, M. D., 257(96), 262
White, A. M., 50(80), 55
White, F. H., 171(49), 799
White, F. H., Jr., 209(21), 224(21),
230(21), 231
White, H. A., 269(25), 274(25), 275(25),
276(25), 283(25), 286, 371(45), 378
White, J. C, 35(11), 36(11), 37(11), 39
(29), 40(11), 41(36), 52, 53
White, J. D., 91(43), 97(43), 102
Whitehead, J. S., 72(118), 81
Whitehead, W. M., 98(91), 103
Whitehouse, J. M., 322(76), 351
Whitelaw, J. W., 22(215), 30
Whitfield, C, 182(114), 201, 317(49),
320(49), 336(49), 337(49), 350
Whitlock, H. W., 371(46), 378
Whitmore, G. F., 345(143), 353
Whittaker,R.H.,2(3),25
Wicks, J. H., 95(63), 97(63), 102
Wide, L., 97(59), 102
Wiegel, J., 174(76), 200
Wieringa, K. T., 167(11, 13), 198
Wilharm,G.,5(24),24
Wilkinson, G. J., 158(31), 163
Willard, H. F., 74(154), 82, 340(123),
241(131),J5J
Williams, A. M., 385(33),415
Williams, D. A., 156(21), 163
Williams, D. C, 339(112), 340(112),
352
Williams, G. R., 176(82), 200
Williams, J. E., 376(71), 379
Williams, M. A., 345(167), 354
Williams, P. M., 8(85, 86), 25, 26
Williams, R., 76(206), 84
Williams, R. J. P., 152(8), 154(8), 155
(16), 156(16), 157(25, 30), 162, 163,
245(50), 261, 315(45), 350
Williams, T. H., 140(47), 141(47), 148
Williams, W. L., 13(143), 27
Wilmanns, W., 17(173), 28, 343(144),
345(166), 353, 354
Wilms, K., 17(173), 28, 243(144), 353
Wilson, J., 7(56), 19(56), 24, 76(194),
84, 88(17), 101, 344(162), 354
Wilson, K. A., 16(170), 28
Wilson, P., 347(190), 355
Wilson, R. M., 290(3, 4, 6), 291(15),
303, 304
Windgassen, R. J., 338(96), 352
Windorski, D. C, 95(63), 97(63), 102
Winfield, M. E., 397(86), 406(86, 105),
407(86), 417, 418
Winkler, M. F., 7(68), 25
Winter, A. R., 5(12), 23
Winzer,K., 167(12), 198
Wise, I. J., 161(53), 164
Withey,J.L.,98(82),70.?
Witkop,B.,91(46),/02
Witt, L., 393(82),417
Witt, L. L., 402(96), 403(96), 417
Witts, L. J., 16(169), 28
Woldring, M. G., 95(115), 104
Wolfe, R. S., 166(6), 167(6), 168
(6, 18), 172(18), 175(18), 177
(94), 178(18), 182(115), 190
(115), 196(6), 198, 201
Womack, M., 340(126), 353
Wong, K. -T. J., 75(175), 83, 89(33),
101
Wood, H. G., 166(7), 169(29, 30),
170(33, 39), 171(29, 33, 39, 44),
172(7, 30), 173(29, 44, 60), 176
(90, 91, 92), 177(91, 92, 95, 96),
178(29, 91, 96, 104, 106), 179(91,
96, 106, 108), 180(91, 108), 182
(90, 92), 183(116, 117), 184(90,
116, 117), 186(118, 119), 187
(121a), 189(106, 119, 121a), 190
(90, 96, 116, 119), 191(96), 192
(33, 39), 193(39), 195(39), 196
(33, 39), 198, 199, 201, 297(25),
304, 338(95), 352, 359(9), 361
(13, 14), 362(17, 19, 20), 363(13),
364(19, 20, 25), 365(13), 366(13),
367(13), 368(31), 377
Wood, J. M., 10(104), 26, 91(36), 101,
152(6, 7, 8, 9, 10, 11, 12), 153(13),
154(8), 155(17, 19), 156(17, 19),
157(27, 28), 158(36), 159(28), 160
(19, 40), 161(12, 17, 45), 162, 163,
164, 177(94), 182(115), 190(115),
201, 267(20), 282(20), 286, 383
(24, 29), 384(24), 386(24), 389(29),
391(24), 415
Wood, P. H. N., 98(82), 103
Wood, T. R., 16(165), 28
Wood, W. A., 234(1), 259
Woodams, A. D., 371(44), 378
Woodrow, M. L., 35(16), 40(16),
41(16), 42(41), 52
Woods, D. D., 11(121, 122), 27, 33(3),
52, 308(3, 4, 6, 7, 9, 10), 309(3, 6, '
20, 23), 317(23), 320(2, 3, 72), 322
(72), 329(23), 339(72, 98), 349,
351, 352
Woodward, R. B., 112(20), 147
Woolley, D. W., 3(10), 23
Wright, A., 48(57, 58), 54, 382(2),
386(2), 414
Wu, R., 157(29), 163
Wu, T. -F., 177(95), 201
Wung, P. T. S., 161(49), 164
Wurm, R., 192(126), 202
Yakovlev, V. A., 254(86 87) , 57(87),
262
Yakusheva, M. I., 254(86, 87), 257(87),
262
Yamada, R., 337(93),
352, 397(86), 406
(86, 106), 407(86), 410(106), 417, 418
Yamada, R. -H., 59(25), 78, 388(68),
417
Yamamoto, R. S., 12(129), 27
Yamane, T., 239(19), 243(19), 251(74),
260, 262
Yang, L. Y., 389(73), 417
Yang, S. -S., 173(57), 174(76), 184(57),
191(124), 199, 200, 202
Yanofsky, C, 42(44), 53
Yansura, D. G., 108(13), 121(13), 147
Yap, T., 393(82), 417
Yau, S., 384(20), 386(20), 389(20), 393
(20), 415
Yeh, Y. :., 389(72), 417
Yemm, E. W., 229(49), 232
Yeung, C. Y., 389(73), 417
Yki-Jarvinen, H., 71(97), 72(97), 80
Yollnshaw, E. M., 156(23), 163
Youngdahl-Turner, P., 74(148, 154, 155),
82, 83 , 88(13), 100, 340(123), 353
Yoshiba, K., 33 9(117), 342(11 7), 352
Yurkevich, A. M., 91(40), 102, 158
(32, 35), 163
Zagalak, B., 239(18), 243(18, 40), 253
(79), 254(79), 259, 260, 262(16), 263
(16), 264(16), 265(16), 266(16), 267
(16), 269(37), 370(39), 371(30), 372
(54,61), 373(37), 377, 378
Zak, Z., 4(11), 23
Zalusky, R., 76(195), 84, 344(153), 354
Zamcheck, N., 35(12), 48(12), 52
Zappia, V., 205(8, 9), 230
Zeylemaker, W. P., 372(51), 378
Zittoun, J., 20(193), 29, 76(201, 209),
84
Zittoun, R., 20(193), 29, 76(201), 84
Zondag, H. A., 91(45), 102
Zubay, G., 257(98), 262
Zuber, C, 75(185), 83
Zucker, L. M., 6(43), 24
Zucker, T. F., 6(43), 24
Subject Index
Abnormal dU suppression, methionine
synthetase, methylcobalamin,
345
Absence, receptor Escherichia coli
cobalamins, 36
Absorption spectra, see Electronic
spectrum
Absorption vitamin B 12 , human, 12
Acceptor binding calcium, intrinsic
factor, 71
Acceptor-cobalamin complex, Stokes
radii intrinsic factor, 72
Acceptors, calcium transcobalamin,
74
Accuracy, cobalamin quantitation,
89
Acetate:
methane cycle, 166
methyl group from carbon dioxide,
177
Acetate biosynthesis:
acetogenic bacteria:
carbon dioxide, 167
Clostridium aceticum, 167
formate dehydrogenase, 173
acetoxycorrinoid mechanism, 179
bicarbonate, 167
carbohydrate-fermenting bacteria,
168
from carbon dioxide and hydrogen,
168
carbon monoxide and methyltetrahydrofolate, 187
purified components, 188
purines, 193
carboxymethylcobalamin, 179
carboxymethylcorrinoid mechanism,
179
cecal, 167
cellulose, 168
corrinoid pathway, 172
Embden-Meyerhof pathway, 169
Entner-Doudoroff pathway, 170
ferridoxin oxidoreductase, 173
formate dehydrogenase, 172
formate as intermediate, 168
formyltetrahydrofolate synthetase,
173,174
glucose, 169
glycine, 170,194
glycine decarboxylase Peptococcus
streptococcus, 194
glycine decarboxylation, noncorrinoid, 192
Grignard mechanism, 179
guanine, 170
hydrogen, electron source, 167
hypoxanthine, 170
intrinsic factor inhibition, 177
mechanism of Clostridium thermoaceticum, 181
methenyltetrahydrofolate cyclohydrolase, 173,174
methylcarbanion mechanism, 179
CD 3 -methylcobalamin, 179
methylcobalt corrinoids, 166
methy lcorrinoids:
Clostridium thermoaceticum, 177
intermediates, 177
pathway mechanism, 179
methylenetetrahydrofolate dehydrogenase, 173,174
methylenetetrahydrofolate reductase, 173
methyl-factor IIIm a-keto acids, 178
CD 3 -methyltetrahydrofolate, 179
purine-fermenting bacteria, 170
pyruvate, 172
role, tetrahydrofolic acids, 174
transcarboxy lation, 173
transmethylase, 173
uric acid, 170
xanthine, 170
see also Acetic acid
Acetic acid:
carboxyl group:
carbon dioxide, 178
pyruvate carboxyl group, 178
transcarboxylation, 178
methylcobalamin incorporation, 177
Acetobacterium woodii:
acetogenic bacteria, 167
t etrahydrofolate enzymes, 176
Acetobacter suboxydans glutamate
mutase, 291
Acetogenic bacteria:
Acetobacterium woodii, 167
Butyribacterium rettgeri, 170
carbon dioxide acetate biosynthesis,
167
Clostridium aceticum acetate biosynthesis, 167
Clostridium acidiurii, 167
Clostridium cylindrosporum, 167
Clostridium formicoaceticum, 167
Clostridium sticklandii, 111
Clostridium thermoaceticum, 167
Diplococcus glycinophilus, 171
electron transport, 196
energy metabolism, 196
Eubacterium limosum, 170
formate dehydrogenase, acetate
biosynthesis, 173
hydrogen, electron source, 167
Methanobacillus kuzneccovii, 171
Peptococcus glycinophilus, 171
stimulation:
ferrous sulfate, 167
folic acid, 167
molybdate, 167
selenite, 167
vitamin B 12 ,167
Acetoxycorrinoid mechanism acetate
biosynthesis, 179
Acid ninhydrin, L-/3-lysine mutase assay,
211
Activation:
S-adenosyl-L -methionine, methionine
biosynthesis, 331
L-b-lysine mutase:
activity, 212
cobalt-carbon bond, 251
El, 215
2 '-O-methyl ATP ribonucleotide
reductases, 402
3 -0-methyl ATP ribonucleotide
reductases, 402
methyl iodide methionine biosynthesis,
331
Activation parameters ethanolamine
ammonia-lyase, 268
Activators, ribonucleotide reductases,
ribonucleotide analogs, 402
Active site:
amino acids diol dehydrase, 241
cysteine diol dehydrase, 241
resistance to free radical attack,
ethanolamine ammonia-lyase,
263-287
thiols, diol dehydrase, 241
Activity:
activation L-j3- lysine mutase,
212
diol dehydrase, vitamin B 12 coenzyme
side chain modification, 247
a-(Iower)-Iigand modification, 248
b-(upper)-Iigand modification, 249
Escherichia coli, Met H mutant effect
of growth media on, 324
glutamate mutase, vitamin B 12 coenzyme
specificity, a-(lower)-Iigand
modification, 294
temperature effect, ribonucleotide
reductases, 400
Activity relationship, diol dehydrase
corrinoid structure, 247
Adenine cobalamins 5,6-dimethylbenzimidazole, 51
Adeninylbutylcobalamin ribonucleotide
reductases, inhibitor constants,
401
Adeninylethylcobalamin ribonucleotide
reductases, inhibitor constants,
401
Adeninylhexylcobalamin ribonucleotide
reductases, inhibitor constants,
401
Adeninylpentylcobalamin ribonucleotide
reductases, inhibitor constants,
401
Adeninylpropylcobalamin ribonucleotide
reductases, inhibitor constants,
401
Adenosine triphosphate, L-/3-lysine
mutase cofactor, 215
Adenosylcobalamin, see Vitamin B 12
coenzyme
L-Adenosylcobalamin ribonucleotide
reductases, inhibitor constants,
401
Adenosylethylcobalamin ribonucleotide
reductases, inhibitor constants,
401
S- Adenosyl- L -homocysteine:
methionine synthetase, 320
priming methionine synthetase, 347
5-Adenosyl-L-homocysteine dependent
propyl iodide methionine
synthetase, 336
S-Adenosyl-L- methionine:
methionine biosynthesis activation,
331
replacement by methyl iodide methionine
synthetase, 329
role, methionine synthetase, 329
S-Adenosyl-L-methionine, methionine
synthetase, methyl iodide replace ment,
329
S- Adenosylmethionine as replacement
vitamin B 12 coenzyme, 206
S- Adenosylmethionine cleavage
pyruvate formate-lyase
Escherichia Coli i 205
S- Adenosylmethionine reversible cleavage
hydrogen carrier, noncorrinoid,
205
7-Adenylhydrogenobamide, 110
9-Adenylhydrogenobamide, 110
Administration, therapeutic use,
vitamin B 12 , 20
ADP, 2'-fluoro analog ribonucleotide
reductases, 412
Adsorption, pernicious anemia,
cobalamins, 72
Aerobacter aerogenes:
diol dehydrase, 233-262
methionine synthetase, 339
ribonucleotide reductases, 383
Affinity chromatography:
cobalamin analogs isolation, 17
cobalamin-binding proteins labile
ligand, 59
cobalamin-binding proteins Sepharose,
60
cobalt-carbon b ond, co nventional
s,
cobalamin-binding protein
table, 64
column preparation cobalamin-binding
proteins, 59
diol dehydrase, 251
immunoprecipitation cobalamin-binding
proteins, 61
labile ligand, 59
ribonucleotide reductases:
ATP-Sepharose, 388
dATP-Sepharose, 388
dGTP-Sepharose, 388
purification, 387
vitamin B 12 coenzyme Sepharose,
388
vitamin B 12 monocarboxylic acid
cobalamin-binding proteins, 60
Aglycone p-cresol factor lb, 5
(2S)-Alaninol structure, 372
Alfalfa, vitamin B 12 , 9
Algae:
ribonucleotide reductases, distribution,
381-418
vitamin B 12 occurrence, 10
Alkali, electronic spectrum, hydrogenobalamin, 114
Alkaline phosphatase, therapeutic use,
vitamin B 12 , serum, 22
Alkali reaction, metal-free corrinoids,
114
Alkylating agent, methionine synthetase
5-methyltetrahydrofolate, 326
Alkylcobalamin as intermediate diol dehydrase, 240
Alkylcobalamins, glutamate mutase
mechanism of action, 297
Alkyl group transfer cobalamins, 3
Alleles, transcobalamin, 73
Allergies, therapeutic use, vitamin B 12 ,
21
Amberlite XAD-2 metal-free corrinoid
purification, 108
Amidation, Lactobacillus leichmannii,
5
Aminoacetaldehyde ethanolamine
ammonia-lyase amino group
migration, 263-287
Amino acid composition:
correlation amongst cobalamin-binding
proteins, table, 68
haptocorrin, 63, 67
intrinsic factor, 63, 67
transcobalamin, 63, 67
Amino acids, diol dehydrase active site,
241-242
Aminoethylcobalamin ribonucleotide
reductases, competitive
inhibitors, 401
Amino group migration:
aminoacetaldehyde ethanolamine
ammonia-lyase, 263-287
Amino group migration (Cont'd)
diamino acid, 206
intramolecular, ethanolamine ammonialyase, 263-287
mechanism of ethanolamine ammonialyase, 263-287
Aminohexyl residue, vitamin B 12 monocarboxylic acids, 38
2-Amino-5-ketohexanoic acid 2,5-diaminohexanoic acid oxidation, 209
2- Amino-4-ketopentanoic acid D-ornithine
mutase Clostridia, 224
d - Aminolevulinic acid, labeled precursors,
corrin ring incorporation, 7
3- Amino-4-methylpentanoic acid, see
|3 -Leucine
Amino mutases:
3,6-deaminohexanoate, 205
b-leucine, 205
leucine-2,3-aminomutase, 205
D-a-lysine, 205
L-b-lysine, 205
L-a-lysine-2,3-aminomutase,
noncorrinoid, 205
D-ornithine, 205
pyridoxal phosphate requirement,
205
1 - Amino-2- propanol:
ethanolamine ammonia-lyase isotope
effects, 263-287
threonine labeled precursors, 7
2-Aminopropanol ethanolamine
ammonia-lyase:
isotope effects, 263-287
stereochemistry, 263-287
(R)- 2- Aminopropanol ethanolamine
ammonia-lyase, 267, 269
(S) -2- Aminopropanol ethanolamine
ammonia-lyase, 267, 269
L-2-Aminopropanol ethanolamine
ammonia-lyase vitamin B 12
coenzyme, 263-287
2-Aminopropanol-1-yl radical ethanolamine
ammonia-lyase, 275
Amino terminal:
cobalamin-binding proteins, 69
haptocorrin, 69
intrinsic factor, 69
transcobalamin, 69
Amino terminal sequence:
cobalamin-binding proteins, purifica-tion,
62
haptocorrin, 66
intrinsic factor, 65
transcobalamin, 66
Ammonia adduct, ethanolamine
ammonia-lyase, formylmethylcobalamin, 263-287
Amniotic fluid haptocorrin, 60
Anabaena flos-aquae ribonucleotide
reductases, cobalamins, 384
Anabena cylindria, vitamin B 12 , 9
Anacystis nidulans ribonucleotide reductases,
cobalamins, 384
Anaerobic organisms, vitamin B 12 coenzyme,
32
Analog binding ribonucleotide
reductases, vitamin B 12 coenzyme,
400
Analogs:
as coenzymes, ribonucleotide
reductases, vitamin B 12 coenzyme,
400
as cofactors, ethanolamine ammonialyase, vitamin B 12 coenzyme,
267
as inhibitors, ribonucleotide
reductases, vitamin B 12 coenzyme,
400
methylmalonyl-CoA mutase, vitamin B 12
coenzyme, 366
rhodibalamin s vitamin B 128 ,
130
vitamin B 12 coenzyme, 400
Analysis, see Assay
Antagonists, intrinsic factor, decreased
production, histamine-H 2 receptor
71
Antibody:
cobalamin-binding proteins, 70
cobalamins, isotope dilution assay, 95
transcobalamin, 75
Antihaptocobalamin, cobalamin-binding
proteins, 70
Antimetabolite properties:
hydrogenobalamin:
Escherichia coli, 139
Lactobacillus leichmannii, 139
metal-free corrinoids, 139
methylrhodibalamin, 139
vitamin B 12 metal analogs, 139
Antimony(III), methylcobalamin reaction,
155
Antiquity, vitamin B 12 evolutionary, 2
Antitranscobalamin, cobalamin-binding
proteins, 70
Apoenzyme:
electronic spectrum methionine
synthetase, 311
regulation diol dehydrase, 257
Appearance, vitamins, evolutionary, 2
Appetite stimulant, therapeutic use,
vitamin B 12 , 21
Aqueous humor, human, cobalamin
distribution, 16
AquoCbl,see Aquocobalamin; Hydroxocobalamin
Aquocobalamin:
complex:
with haptocorrin, cobalamins, 70
with intrinsic factor, cobalamins, 70
with protein-histidine, 91
with transcobalamin, cobalamins, 70
conversion, vitamin B 12 , 91
60
Co-labeled, 92
methylcobalamin haptocorrin conversion
to, 90
stannous reduction, 155
vitamin B 12 coenzyme haptocorrin
conversion, 90
see also Hydroxocobalamin
Aquoferribalamin electronic spectrum,
138
Aquorhodibalamin electroni
c
spectrum,
130,131
Arabino adenosylcobalamin ribonucleotide
reductases, inhibitor constants, 401
Arabino ATP ribonucleotide reductases:
inhibition, 402
nucleotide analogs, 403
Arabino CTP ribonucleotide reductases,
nucleotide analogs, 403
Archaic anaerobes, vitamin B 12 occurrence,
2
Aristeromycylcobalamin ribonucleotide
reductases, inhibitor constants,
401
cobalamins,
Arsenate, Escherichia coli
effect of, 44
Arthrobacter glo biformis,
glycine biosy nthesis me
thylenetetrahydrofolate,
195
Arthrobacter sp. (No. 38), vitamin B 12
exogenous nutrient, 11
Asialo acceptors, haptocorrin, 76
Assay:
acid ninhydrin, L-j3-lysine mutase, 211
colorimetric assay, ribonucleotide reductases, 390
comparison of methods, ribonucleotide
reductases, 391
diol dehydrase, 233-262
electrophoresis, L-/3-lysine mutase, 213
fluorometric ribonucleotide reductases,
391
glutamate mutase, 291
Lactobacillus lactis Dorner cobalamins,
6
L-leucine-2,3-aminomutase, 229
[5-14C] methyltetrahydrofolate methionine
synthetase, 310
microbiological assay, methionine
synthetase, 309
organoborate-linked insoluble supports,
ribonucleotide reductases, 389
plasma cobalamins, 17
R-protein cobalamins, 17
radioisotope assay, ribonucleotide
reductases, 389
radiotracer method, methionine
synthetase, 310
ribonucleotide reductases, [5'-3 H] vitamin B 12 coenzyme, 390
spectrophotometric assay:
L-/3-lysine mutase, 211
methylmalonyl-CoA mutase, 364
D-ornithine mutase, 225
ribonucleotide reductases, 390
thin layer chromatography:
L-/3-lysine mutase, 213
D-ornithine mutase, 226
thioredoxin reductase, ribonucleotide
reductases, 390
16
tissue cobalamins,
tritium exchange, assay ribonucleotide
reductases, 390
vitamin B 12 , microorganisms, 7
Astasia Ionga y ribonucleotide reductases,
cobalamins, 384
ATP:
deoxynucleoside triphosphate binding
ribonucleotide reductase, 396
ribonucleotide reductases:
nucleotide analogs, 403
r elative rates of reduction, 393
ATP-Sepharose, affinity chromatography,
ribonucleotide reductases, 388
Autoimmune disease transcobalamin, 20
Autotrophs, 2
AUXBI CHO cells, 343
Axial ligand exchange rhodium corrinoids,
134
Azidocobalamin complexed with cobalaminbinding proteins, electronic
spectrum, 69
Azobacter vinelandii, vitamin B 12 exogenous
nutrient, 11
B 12 methyltransferase, see Methionine
synthetase
Baboon, vitamin B 12 requirement, 12
Bacillus megaterium:
cobalamin transport, 49
vitamin B 12 exogenous nutrient, 11
Bacillus megaterium KM ribonucleotide
reductases, cobalamins, 384
Bacillus subtilis cobalamin transport, grampositive bacteria, 48
Baceteia ribonucleotide reductases,
distribution, 381-418
Bacteriocins, 39
Bacteriophage BF23:
cobalamin receptor Escherichia coli,
39
cobalamins, 48
Bacteriophage Tl Ton B gene product,
iron chelate transport, 42
Bacteriostatic effect, haptocorrin, 76
Base incorporation:
benztriazoles, corrinoids, 5
4,5-dimethylbenzimidazole, corrinoids,
5
microorganisms, corrinoids, 5
naphthimidazole, corrinoids, 5
phenazines, corrinoids, 5
purines, corrinoids, 5
quinazolines, corrinoids, 5
Base-on, base-off:
methylcobalamin reaction, 154
pKa:
methylcobalamin, 91
vitamin B 12 coenzyme, 91
Base titration, electronic spectrum:
hydrogenobyric acid, 118
yellow hydrogenobyric acid, 119
Beef, vitamin B 12 content, 14
Before porphyrins, vitamin B 12 occurrence,
2
Benzimidazoleribosylcobalamin
ribonucleotide reductases,
inhibitor constants, 401
a - Benzimidazolylhydrogenobamide
structure, 111
Benztriazoles corrinoids, base incorporation, 5
Betaine L-homocysteine iS-methyltransferase, 341
Bicarbonate, acetate biosynthesis, 167
Bile (human):
cobalamin distribution, 16
haptocorrin, 60
Bilirubin, therapeutic use, vitamin B 12
plasma, 21
Binder protein, cobalamins isotope
dilution assay Lactobacillus
leichmannii, 95
R-Binder, 58
Binding:
cobalamins, cell-surface, 32
ethanolamine ammonia-lyase vitamin B 12
coenzyme, 263-287
glutamate mutase subunit vitamin B 12
coenzyme, 298
intrinsic factor metal -free corrinoids
inhibition vitamin B 12 ,141
size change, cobalamins, 71
VitaminB 12 inhibition, 141
methionine synthetase 5-methyltetrahydrofolate, 325
ribonucleotide reductases, allosteric
modifiers, deoxyribonucleoside
vitamin B 12 coenzyme, 395
Binding capacity:
transcobalamin I, 14
transcobalamin II, 14
Binding constant cobalamins, Escherichia
coli, 35
Binding proteins:
cobalamin isotope dilution assays,
95
nomenclature, cobalamins, 58
plasma, vitamin B 12 ,14
Binding site, cobalamin ribonucleotide
reductases, allosteric modifiers,
395
Bioautography, vitamin B 12 , 7
Biochemical role:
diol dehydrase, 255
glycerol dehydrase, 255
L-leucine-2,3-aminomutase, 228
L-|3-lysine mutase, 208
D-ornithine mutase Clostridia,
224
ribonucleotide reductases, 385
Biological distribution, methyltin,
161
Biological fluids occurrence (table),
cobalamin-binding proteins, 60
Biological function, methylmalonyl-CoA
mutase, 357-379
Biological mercury methylation, 152
Biological properties, metal-free
corrinoids, 139-142
Biomethylation tin, 161
Biosynthesis:
cobalt incorporation, vitamin B 12 , 144
deoxyribonucleotide, 386
Gossio's gas trimethylarsine, 151
methylcobalamin, methionine, 155
Rhizobium meliloti, vitamin B 12
coenzyme, 9
role, metal-free corrinoids, vitamin B 12 ,
143
Biosynthetic precursor:
18-dehydro-l 7-desmethylhydrogenobyrinic acid, vitamin B 12 ,
145
metal-free vitamin B 12 ,145
2,2-Bis(aralkyloxycarbonyl)propylcholestanocobaloxime:
methylmalonyl-CoA mutase model
studies, 374
structure, 375
5,15-Bisdesmethylhydrogenobyrinic acid
hexamethyl ester c-dimethylamide:
electronic spectrum, 113
structure, 113
2,2-Bis(ethoxycarbonyl)ethylcobalamin:
methylmalonyl-CoA mutase model
studies, 374
structure, 375
2,2-Bis(ethoxycarbonyl)propylcobalamin
structure, 375
2,2-Bis(ethoxycarbonyl)propylcobaloxime:
methylmalonyl-CoA mutase model
studies, 374
structure, 375
Bismuth(III) methylcobalamin reaction,
155
Blood cells, human, cobalamin distribution, 16
Blue hexacarboxylic acid:
cobalt insertion, hydrogenobyrinic
acid c-amide, 125
electronic spectrum, 126
mass spectrum, 125
NMR spectrum, 125
Body fluids, human, cobalamin distribu tion, 16
Bone marrow, human, cobalamin distribution, 16
Bone marrow aspirate, therapeutic use,
vitamin B 12 , 21
Bone marrow morphological changes,
comparison to vitamin B 12
deficiency, nitrous oxide, 347
Bone marrow vitamin B 12 metal analogs,
141
Bound cobalamin transfer to intrinsic
factor haptocorrin, 71
Brain, human, cobalamin distribution,
16
Bridged cobaloxime structure, 375
8-BromoATP ribonucleotide reductases,
nucelotide analogs, 403
10-Bromovitamin B 12 coenzyme activity,
diol dehydrase, 247
BtuB gene cobalamins, Escherichia coli,
35
1,2-Butanediol, diol dehydrase, substrate
specificity, 239
d-2,3-Butanediol, diol dehydrase,
substrate specificity, 239
meso-2,3-Butanediol, diol dehydrase
substrate specificity isobutylene
glycol, 239
Buttermilk, vitamin B 12 ,14
Butyribacterium rettgeri:
acetogenic bacteria, 170
cobalamin microorganisms, 4
Butyric acid, 3,5-diaminohexanoic acid
conversion to, 208
Calcium:
intrinsic factor acceptor binding, 71
transcobalamin acceptors, 74
Calcium dependent transfer:
microsomes, vitamin B 12 R-protein,
18
mitochondria, vitamin B 12 R-protein,
18
Calibration standards:
cobalamin quantitation, 92
60
Co-Iabeled cobalamins, 92
Camembert cheese, vitamin B 12 ,14
Capped cobaloxime structure, 375
Carbohydrate composition:
haptocorrin, 63, 67
intrinsic factor, 63, 67
transcobalamin, 63, 67, 73
Carbohydrate-fermenting bacteria, acetate
biosynthesis, 168
Carbon dioxide:
acetate, methyl group from, 177
Carbon dioxide (Cont'd)
acetate biosynthesis, acetogenic bacteria,
167
acetic acid carboxyl group, 178
hydrogen, acetate biosynthesis from,
168
hydrogen, acetate biosynthesis from,
168
reduction, formate, 173
Carbon monoxide:
enzyme oxidation, 186
exchange with acetyl-CoA, 188
C-1 precursor of acetyl-CoA, 188
Carbon monoxide and methyltetrahydrofolate, acetate biosynthesis, 187
Carbon monoxide dehydrogenase:
nickel enzyme, 186
relationship to corrinoid enzyme, 189
Carboxyl group:
acetic acid carboxyl group, pyruvate,
178
carbon dioxide acetic acid, 178
transcarboxylation acetic acid, 178
Carboxymethylcobalamin, acetate biosynthesis, 179
Carboxymethylcorrinoid mechanism,
acetate biosynthesis, 179
Carcinoma cells, haptocorrin origin,
hepatic, 75
Carcinoma transcobalamin:
gastrointestinal, 20
metastatic breast, 20
Catalytic:
dithioerythritol methionine synthetase,
317
dithiothreitol methionine synthetase,
317
FADH 2 methionine synthetase, 317
2-mercaptoethanol methionine
synthetase, 317
reducing systems, methionine synthetase,
317
Catalytic cycle, diol dehydrase, 246
Catalytic properties:
L-b-lysine mutase, 213
methionine synthetase, 316
D-ornithine mutase, 226
Catalytic protein, L-b-lysine mutase, E1
protein, 209
Cbi, see Cobinamide
Cbl, see Cobalamins
CDP, 2 - fluoro analog ribonucleotide
reductases, 412
CD spectrum:
cobalamin-binding proteins, 69
ethanolamine ammonia-lyase, 263-287
propylcobalamin, 316
propylcobalamin enzyme methionine
synthetase, 315
propylcobinamide enzyme methionine
synthetase, 315
Cecal, acetate biosynthesis, 167
Cell omQlopc,Escherichia coli Kl2
strains, 33, 35
Cell envelope structure, Escherichia coli,
33
Cell surface binding cobalamins, 32
Cellulose, acetate biosynthesis, 166-202
Cell uptake cobalamins, 32
Cerebrospinal fluid, human, cobalamin
distribution, 16
Chemical properties:
methylmalonyl-CoA mutase, 365
ribonucleotide reductases, 391
Chemical studies L-0-lysine mutase,
220
Chicken binder, protein cobalamins,
isotope dilution assay, 95
Chicken breast, vitamin B 12 , 14
Chicken liver, vitamin B 12 , 14
Chlorella vulgaris, vitamin B 12 , 9
Chloroacetaldehyde, diol dehydrase
inactivation, 240
2 '-Chloro-2 '-dioxyuridine diphosphate
degradation uracil, ribonucleotide
reductases, 412
Chlorodifluoromethylcobalamin,
ribonucleotide reductases,
competitive inhibitors, 401
p-Chlorophenylhydrogenobamide cobalt
insertion, 121
3-Chloro-l,2-propanediol, diol dehydrase
substrate specificity, 239
Chlororhodibalamin, electronic spectrum,
131
10-Chlorovitamin B 12 coenzyme activity,
diol dehydrase, 247
CHO cells, methionine biosynthesis, 343,
345
Choline, ethanolamine ammonia-lyase,
263-287
ChromatiumD methionine synthetase, 339
Chromatium strain D, metal-free corrinoids, 6
Chromatium vinosum, isolation:
p-cresylhydrogenobamide, 108
Chromatium vinosum, isolation (Cont'd)
hydrogenobyric acid, 107
metal-free corrinoids, 107
phenylhydrogenobamide, 107
Chromatography:
cobalamin analogs, isolation affinity
chromatography, 17
cobalamin-binding proteins:
affinity, 59
labile ligand affinity, 59
diol dehydrase affinity, 251
L-b-lysine mutase assay thin layer,
213
methylmalonyl-CoA mut
ase purif
ication, 362
D-ornithine muta se assay thin la yer,
226
R-protein Sepharose affinity, 17
ribonucleotide reductases, purification
affinity, 387
Chromium(II), methylcobalamin reaction
with, 155
Cimitidine, intrinsic factor, decreased
production, 71
Cirrhosis plasma levels, cobalamins,
19
Citrobacter freundii, diol dehydrase, 255
Citrobacter intermedium, diol dehydrase,
255
Clam solids, vitamin B 12 , 14
Classification, vitamin B 12 or metabolite
requirement, microorganisms,
10
Cleavage:
diol dehydrase, cobalt-carbon bond,
244
ethanolamine ammonia-lyase, vitamin B 12
coenzyme, cobalt-carbon bond,
263-287
methionine biosynthesis, cobalt-carbon
bond,338
methylmalonyl-CoA mutase, cobaltcarbon bond, 357-379
Clinical cobalamins:
cobalt-carbon bond, 152
quantitation, 98
Clinical response, therapeutic use,
vitamin B 12 , 21
Clostridia:
2-amino-4-ketopentanoic acid,
D-ornithine mutase, 224
biochemical role, D-ornithine mutase,
224 .
comparison L-b-lysine mutase, table,
D-ornithine mutase, 224
electronic spectrum, D-ornithine mutase,
225
molecular properties, D-ornithine mutase,
225
purification, D-ornithine mutase, 225
pyridoxal phosphate, D-ornithine mutase,
225
Clostridial enzyme ethanolamine, ethanolamine ammonia-lyase, 263-287
Clostridium aceticum, acetate biosynthesis,
acetogenic bacteria, 167
Clostridium acidiurii, acetogenic bacteria,
167
Clostridium cochlearcum, glutamate mutase,
290
Clostridium cylindrosporum, acetogenic
bacteria, 167
Clostridium formicoaceticum:
acetogenic bacteria, 167
corrinoid proteins, unknown function,
190
formate dehydrogenase, 174
tetrahydrofolate enzymes, 176
Clostridium lentopatnesiens, L-Ieucine2,3-aminomutase, 228
Clostridium pasteurianum:
nickel enzyme, 186
non-heme iron formate dehydrogenase,
174
Clostridium sachobutyricum, glutamate
mutase, 290
Clostridium SB4 glutamate mutase,
290
Clostridium sporogenes, L-leucine-2,3aminomutase, 228
Clostridium sticklandii:
acetogenic bacteria, 170
cobalamin microorganisms, 4
L-b-lysine mutase, 209
ribonucleotide reductases, cobalamins,
384
Clostridium sticklandii, glutamate mutase,
290
Clostridium tetani, glutamate mutase,
290
Clostridium tetanomorphum:
cobalamin, 4
b-methylaspartate, glutamate mutase,
290
ribonucleotide reductases, cobalamins,
384
Clostridium thermoaceticum:
acetate biosynthesis:
mechanism of, 181
methylcorrinoids, 177
acetogenic ba cteria, 1 67
cobalamin, 4
corrinoid biosynthesis, 191
corrinoid content, 191
corrinoid proteins, unknown function,
190
factor III, 4
5-methoxybenzimidazole methylcobamide, 177
methylcobyric acid, 177
methylcorrinoid formation, 177
ribonucleotide reductases, cobalamins,
384
tetrahydrofolate enzymes, 176
Clostridum glycolicum, 167
CML-binder, see Haptocorrin
CN-Cbl, see Vitamin B 12
Coated charcoal:
cobalamin separation, 96
extraction of cobalamins, 7
Cobalamins:
absence receptor, Escherichia coli,
36
adsorption, pernicious anemia, 72
alkyl group transfer, 3
Anabaena flos-aquae, ribonucleotide
reductases, 384
Anacystis nidulans, ribonucleotide
reductases, 384
analogs:
detection in plasma, 17
distribution tissue, 17
electronic spectrum, 17
isolation affinity chromatography,
17
placenta, human, 17
R-protein binding, 18
source, 18
aquocobalamin complex:
with haptocorrin, 70
with intrinsic factor, 70
with transcobalamin, 70
assay:
Lactobacillus lactis Dorner, 6
plasma, 17
R-protein, 17
tissue, 16
Astasia longa, ribonucleotide
reductases, 384
Bacillus megaterium KM , ribo nucleotidereductases, 384
bacteriophage BF23, 48
binding proteins:
affinity:
chromatography, 59, 64
immunoprecipitation, 61
vitamin B 12 monocarboxylic
acid, 60
amino acid composition correlation
amongst, 68
amino terminal, 69
antibody, 70
antihaptocobalamin, 70
antitranscobalamin, 70
biological fluids occurrence, table, 60
CD spectrum, 69
cobalamin-binding site, 68
cobalamins complexed with, 70
cobalt-carbon bond, 59
5,6 -dimethylbenzimidazole displacement, 69
function, 68
immunology, 70
intrinsic factor, size change, 71
labile ligand affinity chromatography,
59
purification, table, 62, 64
metal-free cobalamins, 140
names, table, 59
nomenclature, 58
physiology, 70
purification:
amino terminal sequence, 62
Cohn fraction III, 62, 64
purity criteria, table, 62
SDS polyacrylamide, 65
Sepharose-affinity, 60
specificity, Escherichia coli, periplasma, 38
Stokes radii, 67
structure, 63
vitamin B 12 metal analogs, 140
see also Haptocorrin; Intrinsic
factor; R-protein; Transcobalamin
binding site, cobalamin-binding
proteins, 68
calibration standards, crystalline
vitamin B 12 , 60Co-Iabeled, 92
cell uptake, 32
cell-envelope, Escherichia coli , 35
cell-surface binding, 32
Cobalamins (Cont'd)
cirrhosis, plasma levels, 19
Clostridium sticklandii, ribonucleotide reductases, 384
Clostridium tetanomorphum, ribonucleotide reductases, 384
Clostridium thermoaceticum, ribonucleotide reductases, 384
Coccochloris peniocystis, ribonucleotide reductases, 384
complexed with cobalamin-binding
proteins, 70
concentration in serum, 88
conformational change transcobalamin,74
content, human liver, mitochondrial
cobalamins, 16
Corynebacterium nephridii, ribonucleotide reductases, 384
cyanide-free extraction, 16
deficiency distribution, 19
dissociation, cobalamin receptor
Escherichia coli, rate of, 38
distribution:
human, table, 16
in nature, 6
pernicious anemia plasma, 19
effect of arsenate Escherichia coli, 44
electron transport, 3
environmental concentrations, 32
enzyme:
Escherichia coli, 33
reaction, 3
equivalence to colicin binding site
Escherichia coli, 41
Escherichia coli:
binding constant, 35
BtuB gene, 35
cobalt-free corrinoid, 37
cobinamide, 36
corrinoid specificity, 36
lesions, 35
mutants, 35
nucleotide loop, 36
outer membrane, 35
Ton B gene product, 43
Euglena gracilis:
inhibitors, 93
limit of detection, 93
promoters, 93
Euglena gracilis bacillaris, ribonucleotide reductases, 384
Euglena gracilis Z , ribonucleotide
reductases, 384
evolutionary, 1
excretion, human, 12
extraction:
plasma, 89
protein denaturation, 90
serum, 89
use of cyanide, 91
FMNH 2 redox potential, 337
folic acid deficiency, plasma levels, 19
Fremyella diphlosiphon, ribonucleotide
reductases, 384
functional states, Escherichia coli, 41
gram-negative bacteria, 48
haptocorrin bound quantitation, 98
hepatitis plasma levels, 19
from hydrogenobalamin, 120
hypothesis, Escherichia coli, 45
I ndependent methylfolate-homocysteine methyl transferase,
MetHgQne, 33
inner membrane, Escherichia coli, 47
intake, human, 12
intrinsic factor, intestinal uptake, 71
isotope detection:
intrinsic factor, 7
R-protein, 7
isotope dilution assays:
antibody, 95
binding proteins, table, 95
chicken binder protein, 95
commercial kits, 95
comparison to other techniques, 97
dog binder protein, 95
intrinsic factor, 95
Lactobacillus leichmannii binder
protein, 95
nonintrinsic factor, 95
principles, 94
saliva binder protein, 95
toad fish binder protein, 95
theoretical standard curves, 94
transcobalamin, 95
Klebsiella pneumoniae, 48
Lactobacillus acidophilus, ribonucleotide reductases, 384
Lactobacillus leichmannii:
inert cobalamins, 7
[14C] ribonucleotides, DNA
incorporation, 383
ribonucleotide reductases, 93, 384
liver, human, distribution, 16
metal-free corrinoids, transformation,
143
Cobalamins (Cont'd)
microbiological assay:
comparison to other techniques, 97
Escherichia Coli i 93
Ochromonas malhamensis, 93
Micrococcus denitrificans, ribonucleotide reductases, 384
microorganisms:
Butyribacterium rettgeri, 4
Clostridium sticklandii, 4
Clostridium tetanomorphum, 4
Clostridium thermoaceticum, 4
Crithidia fasciculata, 4
Nocardia rugosa, 4
Propionibacterium arabinosum, 4
Propionibacterium freudenreichi, 4
Propionibacterium pentosaceum, 4
Propionibacterium peter ssoni, 4
Propionibacterium shermanii, 4
Propionibacterium technicum, 4
Protaminobacter ruber, 4
Pseudomonas denitrificans, 4
Rhizobium meliloti, 4
Rhodopseudomonas spheroides, 4
Streptomyces aureofaciens, 4
Streptomyces griseus, 4
Strigomonas oncopelti, 4
myelocytic leukemia plasma levels, 19
Nostoc commune, ribonucleotide
reductases, 384
nutrition, human, 12
occurrence:
marine sediments, 8
molds, 5
photosynthetic bacteria, 4
poultry-house litter, 5
rat intestines, 5
sea water, 8
yeasts, 5-10
Ochromonas danica, 50
Ochromonas malhamensis, 50
Oedogonium cardiacum, 50
Oscillatoria prolifera, ribonucleotide
reductases, 384
patterns in disease, 18
patterns in humans, 12
peptidoglycan, Escherichia coli, 47
Phormidium autumnale, ribonucleotide
reductases, 384
Phormidium luridum, ribonucleotide
reductases, 384
Pithomyces chartarum, ribonucleotide
reductases, 384
Plectonema boryanum, ribonucleotide
reductases, 384
propionamide side chain modification
receptor binding, 37
Propionibacterium aeraginosa, 48
Proteus mirabilis, 48
Prototheca zopfi, 50
Pseudomonas stutzeri, ribonucleotide
reductases, 384
quantitation:
accuracy, 89
calibration standards, 92
clinical usefulness, 98
comparison of different assay, 97
different forms, 99
evaluation of method, 88
human serum, 87-104
isotope dilution assays, 94
practicability, 89
precision, 89
reference intervals, 98
specificity, 89
receptor, Escherichia coli:
bacteriophage BF23, 39
colicin E, K, 39
equivalence of receptor function, 39
rate of cobalamin dissociation, 38
release haptocorrin, 75
requirement, Eschericnia coli, 33
Rhizobium japonicum, ribonucleotide
reductases, 384
Rhizobium leguminosarum, ribonucleotide reductases, 384
Rhizobium melilotti, ribonucleotide
reductases, 384
Rhizobium phaseoli, ribonucleotide
reductases, 384
Rhizobium trifolii, ribonucleotide
reductases, 384
ribonucleotide reductases, inhibitors,
381-418
role:
proton motive force, Escherichia
coli, 42
Ton B gene product, Escherichia coli, 42
Salmonella paratyphi, 48
Salmonella typhimurium, 48
Scytonema hofmanni, ribonucleotide
reductases, 384
separation:
coated charcoal, 96
free and protein bound, 96
insolubilized binding protein, 97
Cobalamins (Cont'd)
serum concentration, 89
source in nature, table, 3
Sphaerophorus varius, ribonucleotide
reductases, 384
Synechococcus sp., ribonucleotide
reductases, 384
synthesis, table, microorganisms, 4
synthesis, unidentified microorganisms, 6
therapeutic use, 20
Thermus aquaticus, ribonucleotide
reductases, 384
Thermus X-I, ribonucleotide reductases,
384
transcobalamin bound quantitation, 98
transport:
Bacillus megaterium, 49
Escherichia coli, 33, 43
Eucaryotic, 50
gram-positive bacteria:
Bacillus Subtilis i 48
Lactobacillus delbrueckii, 48
Lactobacillus leichmannii, 49
peptidoglycan, 48
microorganisms, 31
Ton B gene product, 43
transport, table, Escherichia coli
mutant strains, 35
undetected by microbiological
assay, 17
see also Corrins; VitaminB 12 ; Vitamin
B 12 Coenzyme
Cobalophilin, 58
Cobalt:
deficient Rhizobia, 386
incorporation, vitamin B 12 biosynthesis,
144
methylmalonyl-CoA mutase mechanism
of action, 376
sheep, 12
Cobalt-binding proteins, glycoproteins, 65
Cobalt-carbon bond:
activation, diol dehydrase, vitamin B 12
coenzyme, 251
cleavage:
diol dehydrase, 244
ethanolamine ammonia-lyase, vitamin
B 12 coenzyme, 263-287
methionine biosynthesis, 338
methylmalonyl-CoA mutase, 357379
reaction pathways, 152
cobalamin-binding proteins, 59
free radical attack, methylcobalamin, 155
heterolytic, methylcobalamin, 153
homolytic, methylcobalamin, 153
methylcobalamin, electrophilic attack,
154
nucleophilic attack, methylcobalamin,
160
outer sphere interactions with corrin
ring, 156
oxygen, diol dehydrase inactivation,
240-241
redox-switch methylcobalamin, 153
ribonucleotide reductases:
mechanism of action, 410
VitaminB 12 coenzyme, 408, 410
Cobalt-containing corrinoids, photo tropic
bacteria, metal-free corrinoid
relationship to, 146
Cobalt-free corrinoid cobalamins,
Escherichia coli, 37
Cobalt insertion:
p -chlorophenyIhydrogenobamide, 121
p-cresylhydrogenobamide, 121
hydrogenobalamin, 120
hydrogen obinamide, 120
hydrogenobinamide phosphate, 120
hydrogenobyric acid, 120
hydrogenobyrinic acid 0,c-diamide, 122
hydrogenobyrinic acid c-amide blue
hexacarboxylic acid, 121, 125
metal-free, 117
2-naphthylhydrogenobamide, 121
phenylhydrogenobamide, 121
Cobalt removal, vitamin B 12 , 106
Cobamide protein, L-|3-lysine mutase, El
protein, 209
Cobamides microbiological assay, 93
Cobinamide:
cobalamins, Escherichia coli, 36
from hydrogenobinamide, 120
metal-free corrinoids, transformation,
143
microbiological assay, 93
to vitamin B 12 coenzyme, Escherichia
coli, 5
Cobinamide phosphate, from hydrogenobinamide phosphate, 120
Cobyric acid, from hydrogenobyric acid,
120
metal-free corrinoids, transformation,
143
Cobyrinic acid a,c-diamide, X-ray
structure, 132
Cobyrinic hexamethylester c-lactone
structure, 122
Coccochloris peniocystis, ribonucleotide
reductases, cobalamins, 384
Coenzyme activity, diol dehydrase:
10-bromovitamin B 12 , 247
10-chlorovitamin B 12 , 247
13-epi vitamin B 12 , 247
Cofactor:
adenosine triphosphate, L-jS-lysine
mutase, 215
dithiothreitol:
L-0-lysine mutase, 219
D-ornithine mutase, 226
divalent cations, L-/3-lysine mutase, 218
magnesium ion, L-0-lysine mutase, 218
manganese ion, L-j3-lysine mutase, 218
mercaptans, L-|3-lysine mutase, 219
monovalent cations, L-b-lysine mutase,
218
pyridoxal phosphate, D-ornithine
mutase, 226
pyruvate, L-0-lysine mutase, 219
vitamin B 12 coenzyme:
L-/3-lysine mutase, 217
D-ornithine mutase, 226
Cohn fraction III, cobalamin-binding
proteins, purification, 62, 64
60
Co-Iabelled:
aquocobalamin, 92
cobalamins, calibration standards, 92
methylcobalamir, 92
vitamin B 12 coenzyme, 92
Colicin binding site, Escherichia coli
cobalamins, equivalence to, 41
Colicin E, K cobalamin receptor,
Escherichia coli, 39
Colorimetric assay, ribonucleotide
reductases, 390
Column preparation, cobalamin-binding
ty chroma
tography,
proteins, affini
59
Commercial kits, cobalamin isotope
dilution assays, 95
Commercial production, microorganisms,
vitamin B 12 , 5
Comparison of different assay cobalamin
quantitation, 97
Comparison of methods, ribonucleotide
reductases assay, 391
Comparison:
to diol dehydrase, table, glycerol
dehydrase, 254
to methylcobalamin levels, Nsmethyltetrahydrofolatehomocysteinemethyltransferase, 17
to L-j3-lysine mutase, hydroxocobalamin,
217
to L-|3-lysine mutase, table, D-ornithine
mutase, 227
to vitamin B 12 deficiency, nitrous oxide,
bone marrow morphological
changes, 347
Comparison to other techniques,
cobalamins:
isotope dilution assay, 97
microbiological assay, 97
Competitive inhibitors:
aminoethylcobalamin, ribonucleotide
reductases, 401
chlorodifluoromethylcobalamin, ribonucleotide reductases, 401
dichlorofluoromethylcobalamin, ribonucleotide reductases, 401
formycinylcobalamin, ribonucleotide
reductases, 401
methylcobalamin, ribonucleotide
reductases, 401
ribonucleotide reductases, 401
Complexed:
with cobalamin-binding proteins,
azidocobalamin, 70
with haptocorrin, electronic spectrum:
hydroxocobalamin, 70
vitamin B 12 , 66, 70
with intrinsic factor, electronic
spectrum:
hydroxocobalamin, 70
vitamin B 12 , 66, 70
with platinum salts, vitamin B 12
coenzyme, 161
with protein-histidine, aquocobalamin,
91
with transcobalamin, electronic spectrum:
hydroxocobalamin, 70
vitamin B 12 , 66, 70
Component E:
glutamate mutase, 291
molecular properties, glutamate mutase,
292
Component F, properties, diol dehydrase,
237-238
Component S:
glutamate mutase, 291
properties, diol dehydrase, 237-238
Component S (Cont'd)
sulfhydryl groups, glutamate mutase,
293
Components (E, S):
function, glutamate mutase, 295
interaction, glutamate mutase, 295
Concentration:
cobalamins, serum, 88
haptocorrin plasma, 75, 89
intrinsic factor, 58
transcobalamin plasma, 73, 89
Conformation:
methionine synthetase, haloenzyme
reconstitution, 313
ribonucleotide reductases, allosteric
modifiers, 397
temperature effect, ribonucleotide
r eductases, 400
Conformational change, transcobalamin
cobalamins, 74
Congentital deficiency:
haptocorrin, 76
transcobalamin, 74
Conservation, methionine, 341
Conversion:
to aquocobalamin, vitamin B 12 Coenzyme,
haptocorrin, 90
to butyric acid, 3,5-diaminohexanoic
acid, 208
to corrinoids, Propionibacterium
shermanii metal-free, 142
to vitamin B 12 , aquocobalamin, 91
to yellow corrinoids, zinc corrinoids,
128
Coordination to rhodium corrinoids, 5,6dimethyIbenzimidazole, 133
Copper corrinoids, 128
Copper insertion, metal-free corrinoids, 128
Coprophagy, source, vitamin B 12 , 12
Corepressor of enzyme synthesis,
ribonucleotide reductases,
deoxyribonucleotide, 399
Cornebacterium nephridii, ribonucleotide
reductases:
allosteric modifiers, 398
purification, 388
Correlation amongst cobalamin-binding
proteins, table, amino acid
composition, 68
Corrinoid biosynthesis, Clostridium
thermoaceticum, 191
Corrinoid c-lactone N-iodosuccinimide
metal-free, 112
Corrinoid content, Clostridium thermoaceticum, 191
Corrinoid enzyme, carbon monoxide
dehydrogenase, relationship to,
189
tl
Corrinoid" enzyme, 182
ansmethyIase, 183
Corrinoid pathway, acetate biosynthesis,
Corrinoid proteins, unknown function:
Clostridium formicoaceticum, 190
Clostridium thermoaceticum, 190
Corrinoids:
base incorporation:
benztriazoles, 5
4,5-dimethylbenzimidazole, 5
microorganisms, 5
naphthimidazole, 5
phenazines, 5
purines, 5
quinazolines, 5
Chromatium vinosum isolation, metalfree, 107
cobalamins, metal-free, 143
cobinamide, metal-free, 143
cobyric acid, metal-free, 143
electronic spectrum, metal-free, 113
13-epi, metal-free, 123
metal-free, 105-149
methyltetrahydrofolate transmethylation, 176
Propionibacterium shermanni, metalfree conversion to, 142
Rhodopseudomonas capsulata:
isolation, metal-free, 110
separation, metal-free, 111
Rhodopseudomonas spheroides isolation:
metal-free, 109
yellow metal-free, 109
vitamin B 12 biosynthesis role, metalfree, 143
zinc incorporation, metal-free, 126
Corrinoid specificity, cobalamins,
Escherichia coli, 36
Corrinoid structure-activity relationship,
table, diol dehydrase, 247
Corrin ring:
-aminolevulinic acid labeled precursors,
cobalt-carbon bond, outer sphere interactions with, 156
distortion, ethanolamine ammonia-lyase,
263-287
Corrin ring (Cont'd)
Escherichia coli, inability to synthesize, 5
porphobilinogen labeled precursors, 7
Corrins, 93
see also Cobalamins, Corrinoids, Vitamin
B 12 , microbiological assay
Corynebacterium nephridii, ribonucleotide
reductases, cobalamins, 384
Corynebacterium simplex, methionine
synthetase, 339
Cottage cheese, vitamin B 12 , 14
p -Cresol factor Ib aglycone, 5
p -Cresylhydrogenobamide:
Chromatium vinosum isolation, 108
obalt insertion, 121
Crithidia fasciculata, cobalamins microrganisms, 4
Crystalline vitamin B 12 , cobalamins,
calibration standards, 92
CTP ribonucleotide reductases, relative
rates of reduction, 393
Cultured cells, 5-methyltetrahydrofolate
homocysteine methyltransferase,
mammalian, 342
Cupribalamin:
ectronic spectrum, 129
ectral properties, 128
Cyanide cobalamins, extraction use of, 91
Cyanide-free extraction, cobalamins, 16
Cyanoquorhodibinamide, electronic
ectrum, 131
Cyanocobalamin, see Vitamin B 12
Cyanoferribalamin, electronic spectrum,
15-Cyano-l,2,2,7,7,12-heptamethylcorrin:
structure, 113
synthesis, 112
X-ray structure, 112
Cyanohydroxorhodibinamide, electronic
spectrum, 131
Cystathionine synthesis, methionine, 340
Cysteine, diol dehydrase, active site,
241-242
Cytosylcobalamin, ribonucleotide
reductases, inhibitor constants,
401
Danish depot preparation, vitamin B 12 ,
20
DATP:
deoxynucleoside triphosphate binding
ribonucleotide reductase, 396
ribonucleotide reductases, allosteric
modifiers, 394
DATP-Sepharose, affinity chromatography, ribonucleotide reductases,
388
DCDP deoxynucleoside triphosphate
binding ribonucleotide reductase,
396
DCTP:
deoxynucleoside triphosphate binding
ribonucleotide reductase, 396
ribonucleotide reductases, allosteric
modifiers, 394
Deamination:
3,5-diaminohexanoic acid, 208
ethanolamine ammonia-lyase stereochemistry, 263-287
Decreased production:
cimitidine, intrinsic factor, 71
gastric juice, intrinsic factor, 71
histamine-H 2 receptor, anatagonists,
intrinsic factor, 71
sialic acid content, intrinsic factor, 71
somatostatine, intrinsic factor, 71
Defects:
haptocorrin, table, 73
intrinsic factor, table, 73
transcobalamin, table, 73
Deficiency:
cobalt, Rhizobia, 386
distribution, cobalamins, 19
haptocorrin, congenital, 76
5 -methyltetrahydrofolate homocysteine
methyltransferase, human, 341
5 -methyltetrahydrofolate megoblastic
anemia, vitamin B 12 , 344
vitamin B 12 , 18
Degradation:
5'-deoxyadenosine, vitamin B 12
coenzyme, 406
epr spectrum, ribonucleotide
reductases, vitamin B 12 coenzyme,
406
haptocorrin, 71, 75
intrinsic factor, 72
pancreatic protease, 18
ribonucleotide reductases, epr vitamin
B 12 coenzyme, 406
transcobalamin, 74
uracil, ribonucleotide reductases, 2'-chloro2'-deoxyuridine diphosphate, 412
vitamin B 12r, vitamin B 1 2 coenzyme,
406
Dehydration, diol dehydrase, glycerol,
239-240
18-Dehydro-17-desmethylhydrogenobyrinic acid:
structure, 145
vitamin B 12 biosynthetic precursor,
145
Demethylation gold salts methylcobalamin,
159
Denaturation cobalamins, extraction
protein, 90
5'-Deoxyadenosine:
diol dehydrase, 244
epr spectrum, ribonucleotide reductases,
408
ethanolamine ammonia-lyase, vitamin
B 12 coenzyme, 263-287
hydrogen carrier, noncorrinoid, 205
reversible formation, ethanolamine
ammonia-lyase, 263-287
vitamin B 12 coenzyme degradation, 406
2'-Deoxyadenosylcobalamin, ribonucleotide
reductases, inhibitor constants, 401
5'-Deoxyadenosyl radical, diol dehydrase,
245
5 '-Deoxyadenosylrhodibalamin, electronic
spectrum, 130, 134
Deoxynucleoside triphosphate binding,
ribonucleotide reductase:
ATP, 396
dATP, 396
dCDP, 396
dCTP, 396
dGTP, 396
dITP, 396
dTTP, 396
GTP, 396
UTP, 396
Deoxyribonucleoside:
dissociation constants, table, ribonucleotide reductases, 396
triphosphates, ribonucleotide reductases,
allosteric modifiers, 394
Deoxyribonucleotide:
biosynthesis, 386
corepressor of enzyme synthesis,
ribonucleotide reductases, 399
DNA replication, ribonucleotide
reductases, 399
Euglena gracilis, growth requirement
in place of, 10
Ochromonas malhamensis, growth
requirement in place of, 10
reduction, ribonucleotide reductases,
385
ribonucleotide reductases, 385
Dependent methyl transfer, vitamin B 12 ,
151-164
Deprotonation, metal-free corrinoids,
115
Dermatologic disorders, therapeutic
use, vitamin B 12 , 21
Descobalt corrinoids, see Metal-free
corrinoids
Detection in plasma, cobalamin
analogs, 17
DGTP:
deoxynucleoside triphosphate binding,
ribonucleotide reductase, 396
ribonucleotide reductases, allosteric
modifiers, 394
DGTP-Sepharose, affinity chromatography, ribonucleotide reductases,
388
Diamino acid, a; -amino group migration,
206
3,6-Diaminohexanoate amino mutases,
203-232
2,5-Diaminohexanoic acid:
D-a-lysine mutase, 206
oxidation, 2-amino-5 -ketohexanoic
acid, 209
3,5-Diaminohexanoic acid:
conversion to butyric acid, 208
deamination, 208
L-erythro-3,5-Diaminohexanoic acid,
L-(3-lysine mutase, 206
2,4-Diaminovaleric acid, D-ornithine
mutase, 206, 223
cis-Diammine dichloroplatinum (II),
inhibition methionine biosynthesis, Escherichia coli,
158
Diaquocobinamide methionine
synthetase, haloenzyme
reconstitution, 313
Dicarboxylic acid, metal-free corrinoids,
Rhodopseudomonas capsulata,
110
Dichlorofluoromethylcobalamin, ribonucleotide reductases, competitive
inhibitors, 401
Dicyanoferribalamin, electronic spectrum,
138
Dicyanorhodibalamin, electronic spectrum,
131
Dicyanorhodibyrinic acid, c,c-diamide, X-ray
rystal structure, 132
18,19-Didehydrocobyrinic acid hexathylester c-amide:
ctronic spectrum, 126
idation, hydrogenobyric acid, 125
ructure, 126
4',5'-Didehy dro-5'-deoxy adenosine,
ribonucleotide reductases, 411
18,19-Didehydrogenobyrinic acid
ucture, 145
Dietary requirements, methionine, 340
Dietary supplement, Epystylis, sewage
udge, 6
Different forms, cobalamin quantitation,
99
Dihydrolipoate, ribonucleotide reductases,
hydrogen donors, 386
N6 -Dimethy lATP, ribon ucleotide reductases, nucleo tide analogs,
403
5,6-Dimethylbenzimidazole:
adenine cobalamins, 51
coordination to rhodium corrinoids,
133
displacement, cobalamin-binding
proteins, 69
5-hydroxybenzimidazole cobalamins,
3, 51
incorporation into hydrogenobalamin,
108
labeled precursors, nucleotide incorporation, 7
2-methyladenine cobalamins, 51
4,5-Dimethylbenzimidazole corrinoids,
base incorporation, 5
Dimethylmercury, mercury methylation, 152
6,7-Dimethyl-8-ribityllumazine labeled
precursors, nucleotide incorpora tion,
7
Diol dehydrase:
Aerobacter aerogenes, 233-262
affinity chromatography, 251
alkylcobalamin as intermediate, 240
amino acids, 241
apoenzyme regulation, 257
assay, 235
biochemical role, 255
10-bromovitamin B 12 coenzyme
activity, 247
catalytic cycle, 246
10-chlorovitamin B 12 coenzyme
activity, 247
Citrobacter freundii, 255
Citrobacter intermedium, 255
cobalt-carbon bond:
cleavage, 244
oxygen, 240-241
component F, properties, 237
component S, properties, 237
corrinoid structure-activity relationship,
table, 247
cysteine, 241
5'-deoxyadenosine, 244
5'-deoxyadenosyl radical, 245
distribution, 255
electronic spectrum, 244
enzyme-coenzyme interaction, 246,
250
13-epivitamin B 12 coenzyme activity,
247
epr spectrum, 245
3-fluoro,l,2-propanediol, 238-239
gel electrophoresis, 237, 238
glycerol:
dehydration, 239
fermentation, 233-262
1,3-propanediol /3-hydroxypropionaldehyde, 234
glycerol dehydrase, comparison to, 254
glycols, 238
haloenzyme, reaction with oxygen, 240
hydrogen transfer isotope effects, 243
hydroxyl group transfer, 242
inactivation:
chloroacetaldehyde, 240
glycerol, 240
glycolaldehyde, 240
oxygen, 240-241
isozymes, 259
Klebsiella pneumoniae, 235, 255
mechanism of action, 242-246
metabolic role, 255
modification, 242
molecular properties, 235-236
monovalent cations, 241
physiology, 253
1,2-propanediol, propionaldehyde, 234
Propionibacterium freundenreichii,
255
reactivation, vitamin B 12 coenzyme,
258
relationship to glycerol dehydrase, 253
stereochemistry:
hydrogen transfer, 243
hydroxyl group transfer, 242
Diol dehydrase (Cont'd)
substrate specificity, table, 239
1,2-butanediol, 239
d ,3-butanediol, 239
d,l-butanediol, 239
3-chloro-l,2-propanediol, 239
1,2-ethanediol, 239
(R)3-fluoro-l,2-propanediol, 239
(R,S)fluoro-l,2-propanediol, 239
(S)3-fluoro-l,2-propanediol, 239
glycerol, 239
isobutylene glycol, meso-2,3butanediol, 239
(R-l,2-propanediol, 239
(R)-l,2-propanediol, 239
(S)-1,2-propanediol, 239
thioglycerol, 239
trifluoropropanediol, 239
subunit:
dissociation, 236
structure, 237-238
thiols, 241
thiols modification, 246
vitamin B 12 coenzyme:
cobalt-carbon bond activation, 251
hydrogen transfer, 243
side chain:
a-(lower)-Iigand modification,
activity, 248
b(upper)-Iigand modification,
activity, 249
modification activity, 247
Diplococcus glycinophilus, acetogenic
bacteria, 170
Displacement cobalamin-binding proteins,
5,6-dimethylbenzimidazole, 69
Dissociation cobalamin receptor,
Escherichia coli, rate of
cobalamins, 38
diol dehydrase subunit, 236
methyltin, 161
Dissociation constants, ribonucleotide
reductases, deoxyribonucleoside,
396
Distortion ethanolamine ammonia-lyase
corrin ring, 263-287
Distribution:
algae, table, ribonucleotide reductases,
381-418
aqueous humor, cobalamins, human, 16
bacteria, table, ribonucleotide reductases,
381-418
bile, human, cobalamins, 16
blood cells, human, cobalamins, table, 16
body fluids, human, cobalamins, table, 16
bone marrow, human, cobalamins, 16
brain, human, cobalamins, 16
cerebrospinal fluid, human, cobalamins, 16
cobalamins:
deficiency, 19
liver, human, 16
diol dehydrase, 255
erythrocytes, human, cobalamin, 16
fungi, table, ribonucleotide reductases,
381-418
glycerol dehydrase, 255
human:
hydroxocobalamin, 16
methy lcobalamin, 16
vitamin B 12 , 16
vitamin B 12 coenzyme, 16
human, table, cobalamins, 16
kidney, human, cobalamins, 16
L-leucine-2,3-aminomutase, 228
leukocytes, human, cobalamins, 16
milk, human, cobalamins, 16
in nature:
cobalamins, 6
vitamin B 12 ,6
pernicious anemia plasma cobalamins, 19
pituitary, human, cobalamins, 16
plasma, human, cobalamins, 16
R-protein, 18
spleen, human, cobalamins, 16
tissue, cobalamin analogs, 17
vitamin B 12 , 19
Disulfide bridges, ribonucleotide
reductases, 393
5,5'-Dithio-bis(2-nitrobenzoic acid) L-0lysine mutase, 221
Dithioerythritol:
methionine synthetase, catalytic, 317
ribonucleotide reductases, hydrogen
donors, 386
Dithiols, ribonucleotide reductases:
hydrogen exchange, 404
mechanistic schemes, 410,414
Dithiothreitol:
L-blysine mutase cofactor, 219
methionine synthetase, catalytic, 317
D-ornithine mutase cofactor, 226
ribonucleotide reductases, hydrogen
donors, 386
DITP, deoxynucleoside triphosphate
binding, ribonucleotide reductase,
396
Divalent cations, L-b-lysine mutase cofactor,
218
DNA incorporation, cobalamin dependence,
Lactobacillus Ieichmannii i [14C]
ribonucleotides, 383
DNA replication:
allosteric modifier, ribonucleotide
reductases, 399
dNTP formation, ribonucleotide
reductases, 399
ribonucleotide reductases, deoxyribonucleotide, 399
DNA synthesis:
allosteric modifiers, ribonucleotide
reductases, 399
dNTP's relative amounts, ribonucleotide
reductases, 399
DNTP formation, ribonucleotide reductases,
DNA replication, 399
DNTP's relative amounts, ribonucleotide
reductases, DNA replication, 399
Dog binder protein, cobalamin isotope
dilution assay, 95
DOM, see Gelbstoff
Dose, therapeutic use, vitamin B 12 , 20
DTPP, ribonucleotide reductases, allosteric
modifiers, 394
DTTP, deoxynucleoside triphosphate
binding, ribonucleotide
reductase, 396
E1component:
activation, L-blysine mutase, 215
inactivation, L-blysine mutase, 213
molecular properties, L-0-lysine mutase,
210
protein, L-j3-lysine mutase, 209
purification, L-/3-lysine mutase, 210
E1E2 complex:
interaction, L-/3-lysine mutase, 213
molecular properties, L-/3-lysine mutase,
210
purification, L-blysine mutase, 209
Effect of arsenate, Escherichia coli
cobalamins, 44
Effect of growth media on activity,
Escherichia coli, Met //-mutant, 324
Effect of ions, ribonucleotide reductases,
391
Egg white, vitamin B 12 , 14
Egg yolk, vitamin B 12 , 14
Electronic spectrum:
aquoferribalamin, 138
aquorhodibalamin, 131
azidocobalamin complexed with
haptocorrin, 69
5,15-bisdesmethylhydrogenobyrinic
acid hexamethyl ester c-dimethylamide, 113
blue hexacarboxylic acid, 126
chlororhodibalamin, 131
cobalamin analogs, 17
cupribalamin, 129
cyanoaquorhodibinamide, 131
cyanoferribalamin, 138
cyanohydroxorhodibinamide, 131
5 -deoxyadenosylrhodibalamin, 134
dicyanoferribalamin, 138
dicyanorhodibalamin, 131
dicyanorhodibinamide, 131
18,19-didehydrocobyrinic acid hexamethyl ester c-amide, 126
diol dehydrase, 244
ethanolamine ammonia-lyase, 276
hydrogenobalamin alkali, 116,117
hydrogenobalamin c-lactam, 113
hydrogenobalamin c-lactone, 113
hydrogenobyric acid base titration,
118
hydroxocobalamin complexed:
with haptocorrin, 70
with intrinsic factor, 70
with transcobalamin
, 70
hydroxorhodibalamin, 131
iron(I)balamin, 138
tein, 210
L-j3-lysine mutase, El pro
manganese corr
inoids, 137
manganibalamin c-lactam
,
137
metal-free corrinoids, 113
methionine synthetase:
apoenzyme, 311
propylcobalamin enzyme, 315
VitaminB 12s, 311,314, 334
methylrhodibalamin, 131, 133
monocyanorhodibalamin, 131
D-ornithine mutase, Clostridia,
225
pheylcupribamide, 129
phenylhydrogenobamide, 114
phenylzincobamide, 127
rhodium corrins, table, 131
Electronic spectrum (Cont'd)
vitamin B 12 complexed:
with haptocorrin, 66, 70
with intrinsic factor, 66, 70
with transcobalamin, 66, 70
yellow cobalt containing corrinoids
to red form, 124
yellow hydrogenobyric acid base titration, 119
zincobyric acid, 126
Electron source, acetate biosynthesis,
hydrogen, 167
Electron transport:
acetogenic bacteria, 196
cobalamins, 3
ribonucleotide reductases, 385
Electrophilic attack cobalt-carbon bond,
mcthylcobalamin, 154
Electrophoresis:
L-j3-lysine mutase assay, 213
mcthylmalonyl-CoA mutase, 367
Electrophoretic mobilities, zincobalamin,
127
Electrophoretic properties:
manganese corrinoids, .137
rhodium corrinoids, 135
Embden-Meyerhof pathway, acetate biosynthesis, 169
Energy metabolism, acetogenic bacteria,
196
Entner-Doudoroff pathway, acetate
biosynthesis, 170
Enterochelin Ton B gene product, ferric,
43
Environmental concentrations,
cobalamins, 32
Enzyme-coenzyme interaction, diol
dehydrase, 246, 250
Enzymes:
cofactor requirement, 185
"corrinoid" enzyme, 182
Escherichia coli cobalamins, 33
methionine biosynthesis, vitamin B 12r ,
337
methionine synthetase, vitamin B 12s , 330,
333
oxidation, carbon monoxide, 186
polyacrylamide gel electrophoresis, 185
purification, 181
reaction cobalamins, 3
specific activity, 183
synthesis, ribonucleotide reductases,
deoxyribonucleotide compressor of, 399
Epimerase methylmalonyl-CoA mutase
methylmalonyl-CoA, 32
Epimerization, methylmalonyl-CoA mutase
methylmalonic acid
, 359
13-Epi metal-free corrinoids, 123
13-Epi vitamin B 12 coenzyme activity diol
dehydrase, 247
Epr spectrum:
diol dehydrase, 245
methylmalonyI-CoA mutase, 357-379
ribonucleotide reductases:
allosteric modifiers, vitamin B 12r ,
397
5 -deoxyadenosyl radical, 412
radical pair formation, 406
relaxed radical pair, 409
vitamin B 12 coenzyme degradation,
406
Epr studies:
ethanolamine ammonia-lyase, 274
vitamin B 12 coenzyme degradation,
ribonucleotide reductases, 406
Epystylis sewage sludge, dietary
supplement, 6
Equilibrium constant, methylmalonyl-CoA
mutase, 367
Equivalence to colicin binding site,
Escherichiacoli cobalamins, 41
Equivalence of receptor function, cobalamin
receptor, Escherichia coli, 39
Erythrocytes, human, cobalamin distribution, 16
Erythropoiesis, therapeutic use, vitamin B 12 ,
22
Escherichia coli:
5-adenosylmethionine cleavage, pyruvate
formate-lyase, 205
antimetabolite properties, hydrogenobalamin, 139
bacteriophage BF23, cobalamin
receptor, 39
binding constant, cobalamins, 35
BtuB gene, cobalamins, 35
cell envelope structure, 33
cobalamins:
absence receptor, 36
cell-envelope, 35
effect of arsenate, 44
Escherichia coli (Cont'd)
enzyme, 33
equivalence to colicin binding site,
41
functional states, 41
hypothesis, 45
inner membrane, 47
microbiological assay, 93
peptidoglycan, 47
rate of periplasmic protein, 45
requirement, 33
role:
proton motive force, 42
Ton B gene product, 42
transport, 33, 43
cobalt-free corrinoid cobalamins, 37
cobinamide to cobalamins, 36
cobinamide to vitamin B 12 coenzyme,
5
colicin E, K co
balamin recep tor, 39
corrinoid specificity, cobalamin s, 36
cis-diammine dichloroplatinum(II)
inhibition, methionine biosynthesis,
158
equivalence of receptor function,
cobalamin receptor, 39
ethanolamine ammonia-lyase preparation,
263-287
growth promotion:
hydrogenobalamin, 139
phcnylhydrogenobamide, 139
inability to synthesize corrin ring, 5
Kl2 strains, cell envelope, 33
lesions cobalamins, 35
lipopolysaccharide, 33
Met E strain, 43
Met H gene product, methionine
synthetase, 322
methionine biosynthesis, 307-355
methionine requirement, 33
methionine synthetase, 310
Met H mutant:
effect of growth media on activity,
324
methionine synthetase, 322
purification, 325
methyl folate-homocysteine methyl
transferase, Met H gene, 33
mutants, cobalamins, 35
mutant strains, cobalamins transport,
table, 35
nucleotide loop cobalamins, 36
outer membrane cobalamins, 35
peptidoglycan, 33
periplasma cobalamin-binding proteins
specificity, 38
pyruvate formate-lyase, 181
rate of cobalamins dissociation, cobalamin
receptor, 38
ribonucleotide reductases, 383
tetrahydrofolate enzymes, 176
Ton B gene product, cobalamins, 43
vitamin B 12 :
microorganisms, 11
uptake, 7,11, 34
1,2-Ethanediol, diol dehydrase, substrate
specificity, 239
Ethanolamine, ethanolamine ammonialyase:
Clostridial enzyme, 263-287
isotope effects, 263-287
[I-3H] Ethanolamine, ethanolamine
ammonia-lyase mechanism of
action, 263-287
Ethanolamine ammonia-lyase:
activation parameters, 268
active site resistance to free radical
attack, 284
amino group migration:
aminoacetaldehyde, 279
intramolecular, 278
mechanism of, 280
(i?)-2-aminopropanol, 267, 269
GS'H-aminopropanol, 267, 269
1-amino-2-propanol, 271
2- aminopropanol-l-yl radical, 275
CD spectrum, 285
choline, 265
Clostridial enzyme, ethanolamine, 266
cobalt-carbon bond cleavage, 273, 284
corrin ring distortion, 285
5 -deoxyadenosinc, reversible formation,
272,274
electronic spectrum, 276
epr studies, 274
Escherichia coli, 264, 268
formylmcthylcobalamin ammonia adduct,
280
function, 283
intrinsic factor inhibition, 264
isopropanolamine, 271
isotope effects:
1- amino-2-propanol, 283
2- aminopropanol, 282
ethanolamine, 281
[5-3H] vitamin B 12 coenzyme, 282
Ethanolamine ammonia-lyase (Cont'd)
Klebsiella aerogenes, 264
mechanism of action:
[l-3H]ethanolamine, 270
hydrogen transfer, 270, 271, 276
[5 '- 3 H] vitamin B 12 coenzyme, 271
modification, 266
molecular properties, 266
monovalent cations, 268
pH, activity, 267
photolysis, 285
physical properties, 267
preparation, Escherichia coli, 265
propionaldehyde, 269
Salmonella typhimurum, 264
stereochemistry:
2-aminopropanol, 269
deamination, 268
structure, 266
substrates, kinetic constants, 267
subunit, 266
sulfhydryl groups, 266
transalkylation mechanism, glycylcobalamin, 280
vitamin B 12r , 274
vitamin B 12s , 278
vitamin B 12 coenzyme:
L-2-aminopropanol, 272
analogs as cofactors, 267
binding, 283
cobalt-carbon bond cleavage, 272
5 '-deoxyadenosyl radical, 264, 272
hydrogen carrier, 271
Ethanolamine deaminase, see Ethanolamine
ammonia-lyase
2-(Ethoxycarbonyl)-2-(ethylthiocarbonyl)
propylcobalamin methylmalonylCoA mutase model studies,
374
structure, 375
Ethylmalonyl-CoA:
deuterated stereo specifically, structure,
373
hydrogen migration, methylmalonylCoA mutase, 357-379
products from reaction, methylmalonylCoA mutase, 374
5-Ethyltetrahydrofolate methionine synthetase, methyl group transfer,
319
5-Ethyltetrahydrohomofolatc methionine
synthetase, methyl group transfer,
319
Eubacterium Umosum, acetogenic bacteria,
170
Eucaryotic cobalamin transport, 50
Euglena gracilis:
growth requirement in place of
deoxyribonucleotide, 10
inhibitors, cobalamins, 93
limit of detection, cobalamins, 93
promoters, cobalamins, 93
ribonucleotide reductases:
allosteric modifiers, 398
properties, 392
purification, 388
vitamin B 12 ,7
Euglena gracilis bacillaris, ribonucleotide
reductases, cobalamins, 384
Euglena gracilis Z, ribonucleotide
reductases, cobalamins, 384
Evaluation of method, cobalamins
quantitation, 88
Evolutionary:
antiquity vitamin B 12 , 2
appearance vitamins, 2
retention, vitamin B 12 coenzyme, 32
vitamin B 12 , 1
Exchange with acetyl-CoA, carbon
monoxide, 188
Exclusive synthesis by microorganisms,
vitamin B 12 ,4
Excretion, human, cobalamins, 12
Extracellular metal-free corrinoids,
109
Extraction:
cobalamin assay, 7
plasma cobalamins, 89
protein denaturation, cobalamins,
90
serum cobalamins, 89
use of cyanide, cobalamins, 91
Extrinsic factor, see Vitamin B 12
Factor A, 9
Factor B, 10
Factor Ib aglycone p-cresol, 5
Factor III:
Clostridium thermoaceticum, 4
5-methoxybenzimidazole, 4
Facus, vitamin B 12 , 9
FADH 2 methionine synthetase, catalytic,
317
Fermentation, diol dehydrase, glycerol,
233-262
Fermentation to methane, methanol, 171
Ferric:
enterochelin Ton B gene product, 43
ferrichrome Ton B gene product, 43
Ferrichrome Ton B gene product, ferric,
43
Ferridoxin oxidoreductase, acetate
biosynthesis, 173
Ferrous sulfate, acetogenic bacteria
stimulation, 167
Fibroblasts, synthesis transcobalamin,
73
Flounder, vitamin B j2 , 14
Fluorescence spectrum, ribonucleotide
reductases:
allosteric modifiers, 397
thioredoxin, 385
Fluorometric ribonucleotide reductases
assay, 391
3-Fluoro-l,2-propanediol, diol dehydrase,
238-239
(R)-3-Fluoro-1,2-propanediol, diol
dehydrase substrate specificity,
239
(RS) -3 -Fluoro-1,2-propanediol, diol
dehydrase substrate specificity,
239
(S) - 3 -Fluoro-1,2-propanediol, diol
dehydrase substrate specificity,
239
FMNH 2 redo x p otential, cobalamins, 33 7
Folic acid:
acetogenic bacteria stimulation, 167
deficiency, cobalamins, 19
plasma levels, cobalamins, 19
therapeutic use, vitamin B 12 serum,
22
Folypolyglutamate synthetase, nitrous
oxide inhibition, 346
Formate:
acetate biosynthesis, 168
carbon dioxide reduction, 173
Formate dehydrogenase:
acetate biosynthesis, acetogenic
bacteria, 172
Clostridium formicoaceticum, 174
Clostridium pasteurianum, non-heme
iron, 174
production:
molybdate stimulation, 173
selenite stimulation, 173
tungstate stimulation, 173
Formycin TP ribonucleotide reductases,
nucleotide analogs, 403
Formycinylcobalamin, ribonucleotide
reductases, competitive inhibitors,
401
Formyl-methenyl-methylenetetrahydrofolate
synthetase, Saccharomyces ce revisiae,
176
Formylmethylcobalamin, ammonia adduct,
ethanolamine ammonia-lyase,
263-287
Formyltetrahydrofolate synthetase, acetate
biosynthesis, 173, 174
Free and protein bound cobalamins, separation, 96
Free radical attack, methylcobalamin,
cobalt-carbon bond, 155
Fremyella diphlosiphon, ribonucleotide
reductases, cobalamins, 384
From:
carbon dioxide, hydrogen, acetate
biosynthesis, 168
carbon monoxide and methyltetrahydrofolate, acetate biosynthesis, 187
hydrogenobalamin, cobalamins, 120
hydrogenobinamide, cobinamide, 120
hydrogenobinamide phosphate, cobinamide
phosphate, 120
hydrogenobyric acid, cobyric acid, 120
5-methyltetrahydrofolate methionine
synthetase, methylcobalamin,
328
purified components, acetate biosynthesis,
188
purines, acetate biosynthesis, 193
FTP ribonucleotide reductases, inhibition,
402
Function:
cobalamin-binding proteins, 68
ethanolamine ammonia-lyase, 263-287
glutamate mutase, components (E, S), 295
haptocorrin, 76
Functional states, Escherichia coli
cobalamins, 41
Fundic mucosa, intrinsic factor physiology,
71
Fungi, ribonucleotide reductases,
distribution, 381-418
Gadus pollackius, vitamin B 12 , 9
Galactose residue, haptocorrin, terminal, 76
Gastric juice, intrinsic factor:
decreased production, 71
purification, 62, 64
quantitation, 72, 60
Gastric mucosa, haptocorrin purification,
62
Gastrointestinal carcinoma, transcobalamin,
20
Gaucher's disease, transcobalamin, 20
Gelbstoff, 8
Gel electrophoresis, diol dehydrase, 237-238
Glucose acetate biosynthesis, 166-202
Glutamate mutase:
Acetobacter suboxydans, 291
assay, 291
Clostridium cochlear cum, 290
Clostridium sachobutyricum, 290
Clostridium SB4, 290
Clostridium stiklandii, 290
Clostridium tetani, 290
Clostridium tetanomorphum, 289
component E, molecular properties,
291
component S:
molecular properties, 292
sulfhydryl groups, 291, 293
components (E, S):
function, 295
interaction, 295
hydrogen transfer isotope effects, 300
kinetic properties, 293
mechanism of action, alkylcobalamins,
302
b-methylaspartate, 290
threo-b-methyl-L-aspartate, 289
[3H-methyl] -/3-methylaspartate, 299
purification, 292
subunit, vitamin B 12 coenzyme binding,
296
vitamin B 12 coenzyme specificity,
a.-(lower)-Iigand modification
activity, table, 294
Glutathione, glutathione reductase,
ribonucleotide reductases,
386
Glycerol:
dehydration, diol dehydrase, 240
diol dehydrase:
nactivation, 240-241
substrate specificity, 239
fermentation, diol dehydrase, 233-262
1,3-propanediol, /3-hydroxypropionaldehyde, diol dehydrase, 233-262
Glycerol dehydrase:
biochemical role, 255
comparison to diol dehydrase, table,
254
diol dehydrase, relationship to, 253
distribution, 255
I nactivation, 254
isozymes, 259
Klebsiella pneumoniae, 254
metabolic role, 255
sulfhydryl groups, 235, 254
Glycerol-hydro-lyase, see Glycerol
dehydrase
Glycine, acetate biosynthesis, 170, 194
Glycine biosynthesis, methylenetetrahydrofolate, Arthrobacter
globiformis, 194
Glycine decarboxylase:
Peptococcus glycinophilus, 194
Peptococcus streptococcus, acetate
biosynthesis, 194
Glycine decarboxylation, noncorrinoid,
acetate biosynthesis, 192
Glycolaldehyde, diol dehydrase
inactivation, 240
Glycols, diol dehydrase, 238-239
Glycoproteins, cobalt-binding proteins,
65
a-Glycosidic linkage, vitamin B 12
occurrence, 3
Glycylcobalamin, ethanolamine ammonialyasc, transalkylation mechanism,
280
Gold salts, methylcobalamin demethylation, 159
Gold(III) melthylcobalamin, one-electron
oxidation, 153
Gossio's gas trimethylarsine:
biosynthesis, 152
Scopulariopsis brevicaulis, 152
Gram-negative bacteria, cobalamins,
48
Gram-positive bacteria:
Bacillus subtilis, cobalamin transport,
48
Lactobacillus delbrueckii, cobalamin
transport, 48
Lactobacillus leichmannii, cobalamin
transport, 49
peptidoglycan, cobalamin transport,
48
Granulocyte, haptocorrin origin, 75
Granulocyte binder, see Transcobalamin III
Granulocyte vitamin B 12 binding protein,
see Haptocorrin
Grignard mechanism acetate biosynthesis,
179
Growth promotion:
hydrogenobalamin:
Escherichia coli, 139
Lactobacillus leichmannii, 139
metal-free corrinoids, 139
pheny lhydrogenobamide:
Escherichia coli, 139
Lactobacillus leichmannii, 139
vitamin B 12 metal analogs, microbial,
139
Growth requirement in place of:
deoxyribonucleotide:
Euglena gracilis, 10
Ochromonas malhamensis, 10
methionine:
Lactobacillus lactis, 10
Lactobacillus leichmannii, 10
Growth stimulation, therapeutic use,
vitamin B 12 , 21
GTP:
deoxynucleoside triphosphate binding,
ribonucleotide reductase, 396
ribonucleotide reductases, relative rates
of reduction, 393
Guanine, acetate biosynthesis, 170
Gymnodinium brevis, vitamin B 12
requirement, 8
Half-life:
ranscobalamin, 74
transcobalamin I, 14
t ranscobalamin II, 14
Haloenzyme reaction with oxygen, diol
dehydrase, 240-241
Haloenzyme reconstitution:
conformation, methionine synthetase,
313
13-epi-methylcobalamin, methionine
synthetase, 313
hydroxycobalamin, methionine
synthetase, 313
methylcobalamin, methionine
synthetase, 313
methylcobinamide, methionine
synthetase, 313
sulfitocobalamin, methionine
synthetase, 313
vitamin B 12 , methionine synthetase,
313
vitamin B 12r , methionine synthetase,
313
vitamin B 12 coenzyme, methionine
synthetase, 313
Ham, cured, vitamin B 12 , 14
Haptocorrin:
amino acid composition, 63, 67
amino terminal, 69
amino terminal sequence 66
amniotic fluid, 60
asialo acceptors, 76
bacteriostatic effect, 76
bile, 60
bound cobalamin transfer to intrinsic
factor, 71
carbohydrate composition, 63, 67
cobalamins:
aquocobalamin complex with, 70
release, 75
congenital deficiency, 76
conversion to aquocobalamin:
methylcobalamin, 90
vitamin B 12 coenzyme, 90
defects, 73
degradation, 71, 75
electronic spectrum:
hydroxocobalamin complexed with,
70
vitamin B 12 complexed with, 66, 70
function, 76
heptatic carcinoma marker, 76
immunology, 70
isoproteins, 75
myeloid leukemia, 76
nomenclature, 58
origin:
granulocytes, 75
hepatic carcinoma cells, 75
red blood cells, 75
saliva, 75
physiology, 75
plasma concentration, 60, 75, 89
purification:
gastric mucosa, 62
hog, 62, 64
human, 62, 64
plasma, 62, 64
quantitation cobalamins, 98
radioimmunoassay, 76
saliva, 60, 71
sialic acid, 76
terminal galactose residue, 76
transcobalamin separation, 75
see also Cobalamin, binding proteins,
receptors, transport
Haptocorrin-free intrinsic factor, hog,
96
Heavy metal methylation, methylcobalamin,
153
Hemoglobin levels, therapeutic use,
vitamin B 12 , 22
Hepatic carcinoma cells, haptocorrin origin,
75
Hepatitis plasma levels, cobalamins, 19
Hepatocytes, R-protein, 18
Hepatoma transcobalamin, 20
Heterolytic methylcobalamin cobaltcarbon bond cleavage, 153
Hexacarboxylic acid metal-free corrinoids,
Rhodopseudomonas capsulata,
110
Histamine, intrinsic factor stimulation,
71
Histamine-H 2 receptor antagonists,
intrinsic factor, decreased
production, 71
Hog:
haptocorrin free intrinsic factor, 96
haptocorrin purification, 62, 64
intrinsic factor purification, 62, 64
Homoacetate-fermenting bacteria, 168
levels in corrinoid pathway, tetrahydrofolate enzymes, 175
Homocysteine:
methionine biosynthesis, propyl
iodide, 307-355
methylation, methionine synthetase,
320
Homocysteine transmethylation,
methionine biosynthesis, methyltetrahydrofolate, 334
Homolytic methylcobalamin, cobaltcarbon bond cleavage, 153
Horse, vitamin B 12 requirement, 12
Human:
absorption, vitamin B 12 , 13
cobalamins:
distribution, 16
excretion, 12
Intake, 12
nutrition, 12
deficiency, 5-methyltetrahydrofolate
homocysteine methyltransferase,
341
haptocorrin purification, 62, 64
hydroxocobalamin distribution, 16
intrinsic factor purification, 62, 64
L-Ieucine 2,3-aminomutase, role, 228
methylcobalamin distribution, 16
serum cobalamins, quantitation, 87-104
transcobalamin:
origin, 73
purification, 62
vitamin B 12 :
distribution, 16
requirement, 13
vitamin B 12 coenzyme distribution,
16
5- Hydro-6 -amino-dihydrocobyrinic acid
pentamethylester
a-amide c-la ctam,
X-ray crystallography, 124
5-Hydro-6-amino-dihydrogenobyrinic acid
tf-amide c-lactam structure, 120
Hydrogen:
acetate biosynthesis from carbon dioxide,
168
electron source:
acetate biosynthesis, 167
acetogenic bacteria, 167
migration methylmalonyl-CoA mutase
ethylmalonyl-CoA, 357-379
Hydrogen carrier:
5-adenosylmethionine, noncorrinoid,
reversible cleavage, 205
ethanolamine ammonia-lyase, vitamin B 12
coenzyme, 263-287
isotope effects, vitamin B 12 coenzyme,
223
L-0-lysine mutase, vitamin B 12 coenzyme,
222
noncorrinoid 5'-deoxyadenosyl radical,
205
Hydrogen donors:
dihydrolipoate, ribonucleotide
reductases, 386
dithioerythritol, ribonucleotide
reductases, 386
dithiothreitol, ribonucleotide reductases,
386
Hydrogen exchange:
dithiols, ribonucleotide reductases,
404
ribonucleotide reductases, vitamin B 12
coenzyme, 404
Hydrogen migration, methylmalonyl-CoA
mutase, vitamin B 12 coenzyme,
368
Hydrogenobalamin:
alkali electronic spectrum, 116, 117
cobalamins from, 120
cobalt insertion, 120
5,6-dimethylbenzimidazole incorporation
into, 108
Hydrogenobalamin (Cont'd)
Escherichia colv
antimetabolite properties, 139
growth promotion, 139
Lactobacillus leichmannii:
antimetabolite properties, 139
growth promotion, 139
metal-free corrinoids, Rhodopseudomonas
capsulata, 110
structure, 107
Hydrogenobalamin c-lactam, electronic
spectrum, 113
Hydrogenobalamin c-lactone, electronic
spectrum, 113
Hydrogenobamide structure, 107
Hydrogenobinamide:
cobalt insertion, 120
cobinamide from, 120
metal-free, Rhodopseudomonas capsulata,
110
structure, 107
Hydrogenobinamide phosphate:
cobalt insertion, 120
cobinamide phosphate from, 120
metal-free corrinoids, Rhodopseudomonas
capsulata, 110
Hydrogenobyric acid:
base titration, electronic spectrum,
118
Chromatium vinosum isolation, 107
cobalt insertion, 120
cobyric acid from, 120
18,19-didehydrocobyrinic acid
hexamethylester c-amide
oxidation, 125
structure, 107
Hydrogenobyric acid a -lactam structure, 112
Hydrogenobyric acid c- lactone structure,
112
Hydrogenobyrinic acid c-amide:
blue hexacarboxylic acid, cobalt insertion, 125
cobalt insertion, 121
Rhodopseudomonas spheroides isolation,
109
Hydrogenobyrinic acid 0,c-diamide:
cobalt insertion, 122
conversion to 5-hydro-6-amino-dihydrogenobyrinic acid a-amide c-lactam,
116
Rhodopseudomonas spheroides
isolation, 109
structure, 120
Hydrogenobyrinic acid structure, 107
Hydrogen transfer:
diol dehydrase:
stereochemistry, 243
vitamin B 12 coenzyme, 243
ethanolamine ammonia-lyase, mechanism
of action, 263-287
isotope effects:
. diol dehydrase, 243
glutamate mutase, 300
pentose, ribonucleotide reductases,
mechanism of action, 402-414
retention of configuration, ribonucleotide
reductases, 403
role, nucleotide substrates, ribonucleotide
reductases, 405
stereochemistry, ribonucleotide reductases,
403
to and from water, ribonucleotide
reductases, 402, 404
Hydroxocobalamin:
competitive inhibitor L-0-lysine mutase,
217
complexed:
with haptocorrin electronic spectrum,
70
with intrinsic factor electronic spectrum,
70
with transcobalamin electronic spectrum,
70
distribution, human, 16
methionine synthetase haloenzyme
reconstitution, 313
occurrence, foodstuffs, 13
therapeutic use, 20
tissue, 15
see also Aquocobalamin
Hydroxorhodibalamin, electronic spectrum,
131
5-Hydroxybenzimidazole cobalamins,
5,6-dimethylbenzimidazole, 51
(-)- 3-Hydroxyisobutanoic acid structure,
methylmalonyl-CoA mutase,
372
Hydroxyl group migration, ribonucleotide
reductases, 409
Hydroxyl group transfer, diol dehydrase
stereochemistry, 242
0-Hydroxypropionaldenyde, diol dehydrase,
glycerol 1,3-propanediol, 234
Hypochromia, therapeutic use, vitamin B 12 ,
22
Hypoxanthine, acetate biosynthesis, 170
IgG complex transcobalamin, 20
Ileal acceptor, intrinsic factor, 7.1
Ileal disease, vitamin B 12 , 19
Ileal synthesis, transcobalamin, 73
Imerslung-Grasbeck's syndrome, 72
Immunology cobalamin-binding proteins,
70
haptocorrin, 70
intrinsic factor, 70
transcobalamin, 70
Immunoprecipitation, cobalamin-binding
proteins, 61
Inability to synthesize corrin ring,
Escherichia coli, 5
Inactivation:
chloroacetaldehyde, diol dehydrase,
240
glycerol, diol dehydrase, 240
glycerol dehydrase, 254
glycolaldehyde, diol dehydrase, 240
L-b-lysine mutase:
El, 213
iodoacetamide, 221
tetranitromethane, 220
oxygen, diol dehydrase, 240-241
Incorporation:
acetic acid, methylcobalamin, 177
hydrogenobalamin, 5,6-dimethylbenzimidazole, 108
vitamin B 12 biosynthesis cobalt, 144
Inert cobalamins, Lactobacillus leichmannii,,
7
Infectious leukocytosis, transcobalamin, 20
Inhibition:
acetate biosynthesis, intrinsic factor,
177
arabino ATP, ribonucleotide reductases,
402
ethanolamine ammonia-lyase, intrinsic
factor, 263-287
folypolyglutamate synthetase, nitrous
oxide, 345
FTP, ribonucleotide reductases, 402
L-leucine-2,3-aminomutase, intrinsic
factor, 228
L-b-lysine mutase, intrinsic factor,
207
methionine biosynthesis, propyl iodide,
182
methionine synthetase, propyl iodide,
316,320, 322,336
methoxybenzimidazolylcobamide,
ribonucleotide reductases, 401
2-methyladen-9-ylcobamide, ribonucleotide reductases, 401
propyl iodide, methionine biosynthesis,
182
ribonucleotide analogs, ribonucleotide
reductases, 402
vitamin B 12 binding, intrinsic factor:
metal-free, 141
vitamin B 12 , 141
Inhibitor constants of coenzyme analogs,
ribonucleotide reductases, 401
Inhibitors:
cobalamins, Euglena gracilis, 93
cobalamins, table, ribonucleotide
reductases, 401
L-j3-lysine mutase, 220
methylmalonyl-CoA mutase, vitamin B 12
coenzyme, 366
vitamin B 12 coenzyme analogs, ribonucleotide
reductases, 400
In nature:
cobalamins:
distribution, 6
source, 3
vitamin B 12 distribution, 6
Inner membrane, Escherichia coli co balamins,
47
Inosylcobalamin, ribonucleotide reductases,
inhibitor constants, 401
Insolubilized binding protein, cobalamin
separation, 97
Insulin intrinsic factor stimulation, 71
Intake, human, cobalamins, 12
Interaction:
glutamate mutase, components (E, S),
295
L-b-lysine mutase El, E2, 213
Interactions with corrin ring, cobalt-carbon
bond, outer sphere, 156
Intermediates, acetate biosynthesis,
methylcorrinoids, 177
Intestinal uptake, cobalamins, intrinsic
factor, 71
Intracellular metal-free corrinoids, 107
Intramolecular:
ethanolamine ammonia-lyase amino
group migration, 263-287
rearrangement, methylmalonyl-CoA
mutase, 368
Intrinsic factor:
acceptor binding, calcium, 71
acceptor-cobalamin complex, Stokes
radii, 72
Intrinsic factor (Cont'd)
amino acid composition, 63, 67
amino terminal, 69
amino terminal sequence, 65
analysis, 72
carbohydrate composition, 63, 67
cobalamins:
aquocobalamin complex with, 70
isotope detection, 7
isotope dilution assays, 95
concentration, 58
decreased production:
cimitidine, 71
gastric juice, 71
Mstamine-H 2 receptor antagonists,
71
sialic acid content, 71
somatostatine, 71
defects, 73
degradation, 72
electronic spectrum:
hydroxocobalamin complexed with,
70
vitamin B 12 complexed with, 66,
70
gastric juice, 60
haptocorrin bound cobalamin transfer
to, 71
hog haptocorrin, free, 96
ideal acceptor, 71
immunology, 70
inhibition:
acetate biosynthesis, 177
ethanolamine ammonia-lyase, 263-287
L-leucine-2,3-aminomutase, 228
L-0-lysine mutase, 207
intestinal uptake, cobalamins, 71
metal-free corrinoids, inhibition vitamin B 12
binding, 141
mucosal cells, 71
nomenclature, 58
pernicious anemia, 57
physiology, fundic mucosa, 71
placenta, lactogenic hormone, 71
plasma, 60
production, 71
purification:
gastric juice, 62, 64
hog, 62, 64
human, 62, 64
quantitation:
gastric juice, 72
radioimmunoassay, 72
release, 71
size change, cobalamin binding, 71
stimulation:
histamine, 71
insulin, 71
pentagastrin, 71
vitamin B 12 :
inhibition, vitamin B 12 binding, 141
metal analogs, 57-85
see also Cobalamin, binding proteins,
receptors, transport
Iodoacetamide inactivation, L-0-lysine
mutase, 221
N-Iodosuccinimide corrinoid c-lactone,
metal-free, 112
Ionic mechanism, ribonucleotide reductases,
mechansim of action, 411
Iridium(IV) methylcobalamin, one-electron
oxidation, 153, 159
Iron, therapeutic use, vitamin B 12 plasma,
21
Iron analog, vitamin B 12s , 138
Iron(I)balamin, electronic spectrum, 138
Iron chelate transport, bacteriophage
Tl Ton B gene product, 42
Iron insertion, metal-free corrinoids, 138
3-Isoadenosylcobalamin, ribonucleotide
reductases, inhibitor constants,
401
Isobutylene glycol, meso-2,3-butanediol,
diol dehydrase substrate specificity,
239
Isobutyric acid, L-leucine-2,3-aminomutase,
227
Isolation:
affinity chromatography, cobalamin
analogs, 17
p -cresylhydrogenobamide, Chromatium
vinosum, 108
hydrogenobyric acid, Chromatium vinosum
107
hydrogenobyrinic acid c-amide,
Rhodopseudomonas spheroides,
109
hydrogenobyrinic acid j,c-diamide,
Rhodopseudomonas spheroides,
109
metal-free corrinoids:
Chromatium vinosum, 107
Rhodopseudomonas capsulata, 110
Rhodopseudomonas spheroides, 109
phenylhydrogenobamide, Chromatium
vinosum, 107
Isolation (Cont'd)
Rhodospirillum rubrum, metal-free corrinoids, 108
yellow metal-free corrinoids, Rhodopseudomonas spheroides, 109
Isopropanolamine, ethanolamine ammonialyase, 263-287
Isopropylideneadenosylcobalamin, ribonucleotide reductases, inhibitor
constants, 401
Isopropylidenebularylcobalamin, ribonucleotide reductases, inhibitor
constants, 401
Isoproteins:
haptocorrin, 75
transcobalamin, 73
Isotope detection:
intrinsic factor cobalamins, 7
R-protein cobalamins, 7
Isotope dilution assays:
antibody cobalamins, 95
binding proteins, table, cobalamins,
95
chicken binder protein cobalamins, 95
cobalamin quantitation, 94
comparison to other techniques,
cobalamins, 95, 97
dog binder factor cobalamins, 95
intrinsic factor cobalamins, 95
Lactobacillus Ieichmannii f binder
protein cobalamins, 95
nonintrinsic factor cobalamins, 95
principles, cobalamins, 94
saliva binder protein cobalamins,
95
theoretical standard curves,
cobalamins, 94
toad fish binder protein cobalamins,
95
transcobalamin cobalamins, 95
Isotope effects:
2-aminopropanol, ethanolamine
ammonia-lyase, 263-287
diol dehydrase, hydrogen transfer,
243
ethanolamine ammonia-lyase,
263-287
glutamate mutase hydrogen
transfer, 298
methylmalonyl-CoA mutase,
vitamin B 12 coenzyme, 369
vitamin B 12 coenzyme, hydrogen
carrier, 223
[5'-3 H] vitamin B 12 coenzyme,
ethanolamine ammonia-lyase,
263-287
Isozymes:
diol dehydrase, 259
glycerol dehydrase, 259
Keto acids, acetate biosynthesis,
methyl-factor IIIm, 178
3-Keto-4-methylpentanoic acid,
L-leucine-2,3-aminomutase,
228
Kidney, human:
distribution, 16
methylmalonyl-CoA mutase
content, 17
Kinetic behavior, ribonucleotide
reductases, 391
Kinetic constants:
ethanolamine ammonia-lyase
substrates, 263-287
methylmalonyl-CoA mutase,
367
Kinetic effects, ribonucleotide
reductases, allosteric modifiers,
395
Kinetic parameters, methionine
synthetase, 321
Kinetic properties, glutamate mutase, 293
Klebsiella aerogenes, ethanolamine
ammonia-lyase, 263-287
Klebsiella pneumoniae:
cobalamins, 48
diol dehydrase, 235, 255
glycerol dehydrase, 254
Km values:
methionine synthetase, 321
ibonucleotide reductase, 392
Kl2 strains, cell envelope, Escherichia coli,
33
Labelled precursors:
1-amino-2-propanol threonine, 7
corrin ring incorporation:
6-amonolevulinic acid, 7
porphobilinogen, 7
nucleotide incorporation:
5.6- dimethylbenzimidazole, 7
6.6- dimethyl-8-ribityllumazine, 7
riboflavin, 7
Libile ligand affinity chromatography,
cobalamin-binding proteins, 59
cobalamin-binding proteins, table, 62
Lactic dehydrogenase, therapeutic use,
vitamin B 12 plasma, 21
Lactobacillus acidophilus, ribonucleotide
reductases, cobalamins, 384
Lactobacillus delbrueckii, cobalamin transport, gram-positive bacteria, 48
Lactobacillus lactis, growth requirement
in place of methionine, 10
Lactobacillus lactis Dorner, cobalamins
assay, 6
Lactobacillus leichmannii:
amidation, 5
antimetabolite properties, hydrogenobalamin, 139
binder protein cobalamins, isotope
dilution a ssay, 95
cobalamins, 93
cobalamin transport, gram-positive
bacteria, 48
growth promotion:
hydrogenobalamin, 139
phenylhydrogenobamide, 139
growth requirement in place of
methionine, 10
inert cobalamins cobalamins, 7
Lactobacillus leichmannii, [14C] ribonucleotides, DNA incorporation,
cobalamin dependence, 383
ribonucleotide reductases:
allosteric modifiers, 394
cobalamins, 384
properties, 392
purification, 381-418
vitamin B 12 microorganisms, 7, 11
c- Lactone, manganese reductive demetalIation 5 Ill
Lamb, vitamin B 12 , 14
Laminaria, vitamin B 12 , 9
Large molecular size binder see Haptocorrin; Transcobalamin
Lead(IV), methylcobalamin reaction,
155
Lead acetate toxicity, 154
Lesions, cobalamins, Escherichia coli, 35
b- Leucine:
amino mutases leucine-2,3-aminomutase,
205
L-Leucine-2,3-aminomutase, 227
L-Leucine-2,3-aminomutase, 203-232
assay, 229
biochemical role, 228
Clostridium lentopatnesiens, 228
Clostridium sporogenes, 228
distribution, 228
intrinsic factor inhibition, 228
isobutyric acid, 227
3-keto-4-methylpentanoic acid, 228
human, 228
b-leucine, 227
molecular properties, 229
physiology, 228
purification, 229
Leucocyte binder, see Haptocorrin
Leukocyte count, transcobalamin, 20
Leukocytes, human, cobalamin distribution,
16
Levels:
cobalamins:
cirrhosis plasma, 19
folic acid plasma, 19
hepatitis plasma, 19
myelocytic leukemia plasma, 19
in corrinoid pathway, tetrahydrofolate
enzymes, homoacetate-fermenting
bacteria, 168, 175
pernicious anemia plasma vitamin B 12 ,
19
Life on earth, origin, 2
a-(lower)-Ligand modification, activity
diol dehydrase, vitamin B 12
coenzyme side chain, 248
b-(upper)-Ligand modification, activity
diol dehydrase, vitamin B 12
coenzyme side chain, 249
a-(lower)-Ligand modification activity,
table, glutamate mutase,
vitamin B 12 coenzyme specificity,
294
Light sensitivity, methionine synthetase,
328
Limit of detection, cobalamins, Euglena
gracilis, 93
Ling, vitamin B 12 , 9
Lipopolysaccharide, Escherichia coli, 33
Liver:
human:
distribution cobalamins, 16
mitochondria cobalamins, content,
16
methylmalonyl-CoA mutase purification,
sheep, 360
transcobalamin, 73
Liver disease, therapeutic use, vitamin B 12 ,
21
Lobster, vitamin B 12 , 14
D-a-Lysine mutase, see L-b-Lysine mutase
L-b-Lysine mutase:
activity activation, 212
assay:
acid ninhydrin, 211
electrophoresis, 213
spectrophotometric assay, 211
thin layer chromatography, 213
biochemical role, 208
catalytic properties, 213
chemical studies, 220
Clostridium sticklandii, 209
cofactor:
adenosine triphosphate, 215
dithiothreitol, 219
divalent cations, 218
magnesium ion, 218
manganese ion, 218
mercaptans, 219
monovalent cations, 218
pyruvate, 219
vitamin B 12 coenzyme, 217
L-erythro-3,5-diaminohexanoic acid, 206
b5,5'-dithio-bis(2-nitrobenzoic acid), 221
E1 component:
catalytic protein, 209
cobamide protein, 209
electronic spectrum, 210
molecular properties, 210
purification, 210
pyridoxal phosphate, 210
E1E2 complex:
molecular properties, 210
purification, 209
E1, E2 interaction, 213
E2 protein:
molecular properties, 211
purification, 211
sulfhydryl protein, 209
E1 protein stabilization, 214
hydroxocobalamin, competitive inhibitor, 217
inactivation, 220
inhibitors, 220
intrinsic factor inhibition, 207
iodoacetamide inactivation, 221
mechanism of action:
pyridoxal phosphate, 221
Schiff-base intermediate, 221
modification, 220
molecular properties, 209
D-ornithine mutase:
Clostridia comparison, 224
comparison to, 227
purification, 209
substrate specificity, 220
sulfhydryl groups, 221
tetranitromethane inactivation, 221
vitamin B 12 coenzyme hydrogen carrier,
222
vitamin B 12 coenzy me requirement, 207
L-b-Lysine-2,3-aminomutase, noncorrinoid
amino mutases, 203-232
D,L-Lysine racemase, 213
Macrophage synthesis, transcobalamin, 73
Magnesium ion:
L-b-lysine mutase cofactor, 218
ribonucleotide reductases, allosteric
modifiers, 395
Magnetic moments, manganese corrinoids,
137
Mammalian:
cultured cells, 5-methyltetrahydrofolate
homocysteine methyltransferase,
342
methionine biosynthesis, 339
methionine synthetase, 339
methylmalonyl-CoA mutase, 358
5-methyltetrahydrofolate homocysteine
methyltransferase occur rence,
339
occurrence, meth ionine sy nthetase, 33 9
properties, 5-methyltetrahydrofolate
homocysteine methyltransferase,
341
purification, 5-methy
ltetrahydrofolate
homocysteine methy
ltransferase,
341
regulation, methionine synthetase, 339
sulfur metabolism, 340
tissue, vitamin B 12 binding methionine
synthetase, 339
tissues, methionine biosynthesis, 307355
Manganese containing corrinoids:
insertion, metal-free, 135
reductive demetallation, metal-free:
c-lactam, 111
c-lactone, 111
Manganese corrinoids:
electronic spectrum, 137
electrophoretic properties, 137
magnetic moments, 137
reactions, 136
reduction, 138
Manganese ion, L-b-lysine mutase cofactor,
218
Manganibalamin c-lactam, electronic
spectrum, 137
Marine animals, vitamin B 12 occurrence, 2
Marine environments, pseudovitamin B 12
occurrence, 8
Marine fishes, vitamin B 12 requirement, 9
Marine phyloplankton, vitamin B 12 require ment,
8
Marine sediments, cobalamins occurrence in,
8
Marine species, vitamin B 12 , 8
Mass spectrum, blue hexacarboxylic acid,
125
Me-CBl, see Methylcobalamin
Mechanism:
of acetate biosynthesis, methylcorrinoids
pathway, 179
of Clostridium thermoaceticum, acetate
biosynthesis, 181
of ethanolamine ammonia-lyase, amino
group migration, 263-287
of methylmalonyl-CoA mutase, 357-379
Mechanism of action:
alkylcobalamins, glutamate mutase, 302
cobalt-carbon bond cleavage, ribonucleotide reductases, 410
cobalt role, methylmalonyl-CoA mutase,
376
diol dehydrase, 242-246
[ 1-3 H] ethanolamine, ethanolamine
ammonia-lyase, 263-287
hydrogen transfer:
ethanolamine ammonia-lyase, 263287
pentose ribonucleotide reductases, 402
ionic mechanism, ribonucleotide
reductases, 411
mercaptocobalamin ribonucleotide
reductases, 412
mode of rearrangement, methylmalonylCoA mutase, 367
model systems, methylmalonyl-CoA
mutase, 374
pyridoxal phosphate L-0-lysine mutase,
221
radical-carbonium ion mechanism, ribonucleotide reductases, 412
radical mechanism, ribonucleotide
reductases, 413
role, dithiol ribonucleotide reductases,
412
Schiff-base intermediate L-b-lysine mutase,
221
theoretical studies, methylmalonylCoA mutase, 376
vitamin B 12 s , ribonucleotide reductases,
410
[5'-3 H] vitamin B 12 coenzyme, ethanolamine ammonia-lyase, 263-287
Mechanistic schemes:
dithiols, ribonucleotide reductases, 410
ribonucleotide reductases, 409
Mechanistic studies, alkylation with 5methyltetrahydrofolate, methionine
synthetase, 326
Medicago, vitamin B 12 , 9
Megoblastic anemia, vitamin B 12 deficiency,
5-methyltetrahydrofolate, 344
Megoblast to normoblast conversion, therapeutic use, vitamin B 12 , 21
Mercaptans, L-j3-lysine mutase cofactor, 219
Mercaptocobalamin, ribonucleotide
reductases, mechanism of action,
412
2-Mercaptoethanol methionine synthetase:
catalytic, 317
methyl group transfer, 319
Mercuric chloride toxicity, 154
Mercury methylation:
biological, 152
dimethylmercury, 152
methylcobalamin, 152
Metabolic pathway, methylmalonyl-CoA
mutase, Propionibacterium shermanii, 359
Metabolic role:
diol dehydrase, 255
glycerol dehydrase, 255
Metabolic trap, 5-methyltetrahydrofolate,
344
Metal analogs:
antimetabolite properties, vitamin B 12 ,
139
bone marrow, vitamin B 12 , 141
cobalamin-binding proteins, vitamin
B 12 , 140
microbial growth promotion, vitamin
B 12 , 139
Metal-free corrinoids:
alkali reaction, 114
antimetabolite properties, 139
biological properties, 139-142
Chromatium strain D, 6
Chromatium vinosum, 106
cobalamins, cobalamin-binding proteins, 140
Metal-free corrinoids (Cont'd)
cobalt insertion, 117
conversion to corrinoids, Propionibacterium shermannii, 142
copper insertion, 128
corrinoids:
Chromatium vinosum isolation, 107
electronic spectrum, 113
Rhodopseudomonas capsulata:
isolation, 110
separation, 111
Rhodopseudomonas spheroides
isolation, 109
vitamin B 12 biosynthesis role, 143
zinc incorporation, 105-149
corrinoid transformation:
cobalamins, 143
cobinamide, 143
cobyric acid, 143
deprotonation, 115
extracellular, 109
growth promotion, 139
inhibition, vitamin B 12 binding
intrinsic factor, 141
intracellular, 107
N-iodosuccinimide, metal-free corrinoid
c-lactone, 112
iron insertion, 138
Rhodospirillum ru brum,
108
isolation,
c-lactam manganese, reductive demetallation, 111
c-lactone manganese, reductive demetallation, 111
manganese insertion, 135
metal insertion, 117-139
naturally occurring, 106
nomenclature, 107
purification, Amberlite XAD-2, 108
relationship to cobalt-containing
corrinoids, phototropic
bacteria, 146
rhodium insertion, 128
Rhodopseudomonas capsulata:
dicarboxylic acid, 110
hexacarboxylic acid, 110
hydrogenobalamin, 110
hydrogenobinamide, 110
hydrogenobinamide phosphate, 110
pentacarboxylic acid, 110
tetracarboxylic acid, 110
tricarboxylic acid, 107, 110
Rhodopseudomonas palustris, 6, 106
Rhodospirillum rubrum, 6, 106
Streptomyces olivaceus, 6, 107
synthetic, 112
vitamin B 12 , biosynthetic precursor, 145
yellow conversion products, 123
yellow product I, 114
yellow product II, 115
Metal insertion, metal-free corrinoids,
117-139
Metastatic breast carcinoma, transcobalamin, 20
Met E strain, Escherichia coli, 43
Methane, methanol fermentation to, 171
Methane cycle, acetate role, 166
Methanobacillus kuzneccovii, acetogenic
bacteria, 170
Methanobacillus omelianskii, ribonucleotide reductases, 383
Methanol fermentation to methane, 171
Methenyltetrahydrofolate cyclohydrolase,
acetate biosynthesis, 173, 174
Met H gene:
cobalamin-independent methylfolatehomocysteine methyl transferase,
33
Escherichia coli, methyl folate-homocysteine methyl transferase, 33
Met H gene product, methionine
synthetase, Escherichia coli, 322
Met H mutant:
effect of growth media on activity,
Escherichia coli, 324
methionine synthetase:
Escherichia coli, 322
Salmonella typhimurium, 322
purification, Escherichia coli, 325
Methionine:
biosynthesis methylcobalamin, 155
conservation, 341
cystathionine synthesis, 340
dietary requirements, 340
Lactobacillus lactis, growth requirement
in place of, 10
Lactobacillus leichmannii, growth requirement
in place of, 10
nutrition, 340
Methionine biosynthesis:
activation:
S-adenosyl-L-methionine, 331
methyl iodide, 331
CHO cells, 343, 345
cobalt-carbon bond cleavage, 338
Escherichia coli, c/s-diammine dichloroplatinum(II) inhibition, 158, 308
Methionine biosynthesis (Cont'd)
homocysteine, 308
mammalian tissues, 308, 339
methylcobalamin, 309
methyltetrahydrofolate:
homocysteine transmethylation, 334
N-5 methyl group activation, 338
5-methyltetrahydrofolate:
methyl donor, 308
reversible methylation, vitamin B 12s ,
330
5-methyltetrahydropteroyl-L-glutamate
L-homocysteine 5-methyl
transferases, 308
propyl iodide, homocysteine
inhibition, 323
vitamin B 12 dependency, 308
vitamin B 12r enzyme, 337
Methionine requirement Escherichia coli,
33
Methionine synthetase:
5-adenosyl-L-homocysteine dependent
propyl iodide, 336
5-adenosy 1 -L-homocysteine priming,
320,347
5-adenosy 1-L - methionine replacement
by methyl iodide, 329
Aerobacter aerogenes, 339
apoenzyme electronic spectrum, 311
assay:
[5 -14 C] methyltetrahydrofolate, 310
microbiological assay, 309
radiotracer method, 310
catalytic:
dithioerythritol, 317
dithiothreitol, 317
FADH 2 , 317
2-mercaptoethanol, 317
reducing sy stems, 317
catalytic prop erties, 31 6
CD spectrum:
propylcobalamine enzyme, 315
propylcobinamide enzyme, 315
Chromatium D, 339
Corynebacterium simplex, 339
electronic spectrum, 311, 314
Escherichia coli:
Met H gene product, 322
Met //mutant, 310, 322
haloenzyme reconstitution, 311
conformation, 313
diaquocobinamide, 313
13-epi-methylcobalamin, 313
hydroxycobalamin, 313
methylcobalamin, 313
methylcobinamide, 313
sulfitocobalamin, 313
vitamin B 12 , 313
vitamin B 121 ., 313
vitamin B 12 coenzyme, 313
homocysteine methylation, 320
kinetic parameters, 321
Km values, 321
light sensitivity, 328
mammalian:
occurrence, 339
regulation, 339
tissue vitamin B 12 binding, 339
mechanistic studies alkylation with
5-methyltetrahydrofolate, 326
methylcobalamin:
abnormal dU suppression, 345
from 5-methyltetrahydrofolate, 328
methyl group transfer, 318
methyl iodide replacement, S-adenosylL-methionine, 329
5-methyltetrahydrofolate:
alkylating agent, 326
binding, 325
nitrous oxide, 342
Ochromonas malhamensis, 339
physical properties, 310
propylcobalamin enzyme, electronic
spectrum, 315
propyl iodide inhibition, 316, 320, 322,
336
Pseudomonas aeriginosa, 339
Rhizobium meliloti, 339
Rhodopseudomonasspheroides y 339
Rhodospirillum rubrum, 339
Salmonella typhimurium, 339
Salmonella typhimurium Met H mutant,
322
specific activity, 311
Stokes radii, 314
Streptomyces olivaceus, 339
table, 311
vitamin B 12r , 314
vitamin B 12s :
electronic spectrum, 334
enzyme, 330, 333
see also 5-Methyltetrahydrofolate
homocysteine methyltransferase
5-Methoxybenzimidazole methylcobamide:
Clostridium thermoaceticum, 111
factor III, 4
Methoxybenzimidazolylcobamide, ribonucleotide reductases, inhibition,
401
Methycobal, 21
see also Methylcobalamin
2-Methyladenine cobalamins, 5,6-dimethylbenzimidazole, 51
2-Methyladen-9-ylcobamide, ribonucleotide
reductases, inhibition, 401
7-(2-Methyladenyl)hydrogenobamide,
110
9-(2-Methyladenyl)hydrogenobamide, 111
threo-/3-Methyl-L-aspartate glutamate
mutase, 289
b-Methylaspartate glutamate mutase
Clostridium tetanomorphum, 289
(2S, 35)-3-Methylaspartic acid structure,
372
Methylation:
biological, mercury, 152
dimethylmercury, mercury, 152
methionine synthetase, homocysteine,
320
methylcobalamin:
heavy metals, 153
mercury, 152
platinum, 157
thiols, 156
2'-0-Methyl ATP, ribonucleotide reductases,
activation, 402
3'-0-Methyl ATP, ribonucleotide reductases,
activation, 402
Methylcarbanion mechanism, acetate
biosynthesis, 179
Methylcobalamin:
abnormal dU suppression, methionine
synthetase, 345
acetate biosynthesis, CD 3 -methylcobalamin, 179
base-on, base-off pKa, 91
cobalt-carbon bond cleavage:
free radical attack, 155
heterolytic, 153
homolytic, 153
nucleophilic attack, 160
redox-switch, 153
cobalt-carbon bond cleavage reaction
pathways, 152
60
Co-Iabelled, 92
demethylation, gold salts, 159
distribution, human, 16
electrophilic attack, cobalt-carbon bond,
154
13-epi-methylcobalamin, methionine
synthetase, haloenzyme reconstitution, 313
haptocorrin bound conversion to
aquocobalamin, 90
heavy metals, methylation, 153
incorporation acetic acid, 177
mercury methylation, 152
methionine biosynthesis, 155, 307-355
methionine synthetase, haloenzyme
reconstitution, 313
methyl radical transfer, 155
N5 -methyltetrahydrofolate-homocysteine, methyltransferase
comparison to, 17
from 5-methyltetrahydrofolate
methionine synthetase, 328
occurrence foodstuffs, 13
occurrence plasma, 16
one-electron oxidation:
gold(III), 153
iridium(IV), 153
methyl radicals, 153
outer sphere, 153
one-electron reduction, 160
oxidation, iridium(IV), 159
pernicious anemia plasma, 19, 76
photolysis, 90
platinum methylation, 157
reaction:
with antimony (III), 155
base-on, base-off, 154
with bismuth(III), 155
with chromium(II), 155
with lead(IV), 155
with mercury(II), 154
with palladium(II), 155
tetramethyltin, 155
with thallium(III), 155
with tin(III), 155
redox-switch, 157
ribonucleotide reductases, competitive
inhibitors, 401
tetrachloropalladium(II) complex, 157
tetrachloroplatinum(II) complex, NMR
spectrum, 157
thiols, methylation, 156
tissue, 15
Methylcobalt corrinoids, acetate biosynthesis, 166-202
Methylcobinamide, methionine synthetase,
haloenzyme reconstitution,
313
Methylcobyric acid, Clostridium thermoaceticum, 111
Methylcorrinoids:
Clostridium thermoaceticum, acetate
biosynthesis, 177
formation, Clostridium thermoaceticum,
111
intermediates, acetate biosynthesis, 177
mechanism of acetate biosynthesis, 179
Methyl donor, methionine biosynthesis,
5-methyltetrahydrofolate, 307-355
Methylenetetrahydrofolate, ^rtfzrofocfer
globiformis, glycine biosynthesis,
195
Methylenetetrahydrofolate dehydrogenase,
acetate biosynthesis, 173, 174
Methylenetetrahydrofolate reductase,
acetate biosynthesis, 173
Methyl-factor IIIm a-keto acids, acetate
biosynthesis, 178
Methylfolate-homocysteine methyl transferase Met H gene:
cobalamin-independent, 33
Escherichia coli, 33
N5-Methyl group activation, methionine
biosynthesis m
ethyltetrahydrofolate,
338
Methyl group from carbon dioxide, acetate,
177
Methyl group tra
nsfer:
5-ethyltetrahydrofolate, methionine
synthetase, 319
5-ethyltetrahydrohomofolate, methionine
synthetase, 319
2-mercaptoethanol, methionine synthetase,
319
5-methyltetrahydrohomofolate, methionine
synthetase, 318
stereospecificity, methionine synthetase,
318
substrate specificity, methionine synthe tase,
318
Methyl iodide:
methionine biosynthesis activation, 331
replacement S-adenosyl-L-methionine,
methionine synthetase, 329
Methylmalonic acid:
epimerization, methylmalonyI-CoA
mutase, 359
methylmalonic aciduria, methylmalonylCoA mutase, 359
racemase methylmalonyl-CoA mutase,
360
Methylmalonic aciduria:
methylmalonyl-CoA mutase methylmalonic acid, 359
vitamin B 12 , therapeutic use, 21
Methylmalonyl-CoA:
epimerase, methylmalonyl-CoA mutase,
372
structrure, methylmalonyl-CoA mutase,
372
Methylmalonyl-CoA mutase:
assay, spectrophotometric, 364
biological function, 358
chemical properties, 365
cobalt-carbon bond cleavage, 371
content, kidney, human, 17
electrophoresis, 367
epr spectrum, 371
equilibrium constant, 367
ethylmalonyl-CoA deuterated, products
from reaction, 374
ethylmalonyl-CoA hydrogen migration,
369
(-)-3-hydroxyisobutanoic acid, structure,
372
inhibitors, 366
intramolecular rearrangement, 368
kinetic constants, 367
mammalian, 358
mechanism of, 370
mechanism of action:
cobalt role, 376
mode of rearrangement, 367
model systems, 374
theoretical studies, 376
methylmalonic acid:
epimerization, 359
methylmalonic aciduria, 359
racemase, 360
methylmalonyl-CoA:
epimerase, 372
structure, 372
[methyl-2 H3] -me thy lmalonyl-Co A,
368
model studies:
2,2-bis(aralkyloxycarbonyl)propylcholestanocobaloxime, 374
2,2-bis(ethoxycarbonyl)ethylcobalamin,
374
2,2-bis(ethoxycarbonyl)propylcobaloxime, 374
2-(ethoxycarbonyl)-2-(ethylthiocarbonyl)propylcobalamin, 374
modification, 366
Methylmalonyl-CoA mutase (Cont'd)
molecular properties, 365
pernicious anemia, 359
photolysis, 366
physical properties, 365
potatoes, 360
Propionibacterium shermanii, metabolic
pathway, 359
propionic acid metabolism, 358
purification:
chromatography, 362
Propionibacterium shermanii, 361
sheep liver, 360
source, 358
stereochemistry:
rearrangement, 371
retention of configuration, 372
succinyl-CoA, 358
sulfhydryl groups, 366
vitamin B 12 coenzyme:
analogs, 366
content, 366
hydrogen migration, 368
inhibitors, 366
isotope effects, 358, 369
[5'-3H]-vitamin B 12 coenzyme, 370
Methylmercuric chloride toxicity, 154
[3 H-Methyl ] -j3-methylaspartate glutamate
mutase, 299
Methylplatinum(IV), 157
Methyl radicals, methylcobalamin, oneelectron oxidation, 153
Methyl radical transfer methylcobalamin,
155
Methylrhodibalamin:
antimetabolite properties, 139
electronic spectrum, 130, 131, 133
Methyltetrahydrofolate:
acetate biosynthesis, 179
alkylating agent, methionine synthetase,
326
alkylation with 5-methyltetrahydrofolate,
methionine synthetase, mechanistic
synthetase, mechanistic studies,
326
binding methionine synthetase, 325
homocysteine transmethylation,
methionine biosynthesis, 334
megoblastic anemia, vitamin B 12
deficiency, 344
metabolic trap, 344
methyl donor, methionine biosynthesis,
307-355
N-5 methyl group activation, methionine
biosynthesis, 338
methyl trap, 344
[-14 C] methyltetrahydrofolate, methionine
synthetase assay, 309
pernicious anemia, 76
reversible methylation, vitamin B 1 2S
methionine biosyntheis, 330
transmethylation corrinoids, 176
5-Methyltetrahydrofolate homocysteine
methyltransferase:
human deficiency, 341
mammalian:
cultured cells, 342
occurrence, 339
properties, 341
purification, 341
N5 -Methyltetrahydrofolate-homocysteine
methyltransferase, comparison to
methylcobalamin levels, 17
5-Methyltetrahydrohomofolate methionine
synthetase, methyl group transfer,
318
5-Methyltetrahydropteroyl-L-glutamate
methionine biosynthesis, 307-355
Methyltin:
biological distribution, 161
disproportionation, 161
Methyl transfer, vitamin B 12 dependent,
151-164
Methyl trap, 5-methyltetrahydrofolate,
344
Microbial growth promotion, vitamin B 12
metal analogs, 139
Microbiological assay:
cobalamins undetected by, 17, 93
cobamides, 93
cobinamides, 93
comparison to other techniques,
cobalamins, 97
corrins, 93
Escherichia coli cobalamins, 93
methionine synthetase assay, 309
Ochromonas malhamensis cobalamins,
93
vitamin B 12 , 7
Micrococcus denitriflcans, ribonucleotide
reductases, cobalamins, 384
Microorganisms:
assay, vitamin B 12 , 7
Butyribacterium rettgeri cobalamins, 4
classification, vitamin B 12 or metabolite
requirement, 10
Microorganisms (Cont'd)
Clostridium sticklandii cobalamins,
4
Clostridium tetanomorphum cobalamins,
4
Clostridium thermoaceticum cobalamins,
4
cobalamins:
requirement, 32
synthesis, table, 4
transport, 31
corrinoids, base incorporation, 5
Crithidia fasciculata cobalamins, 4
Escherichia coli vitamin B 12 , 11
Lactobacillus leichmannii vitamin B 12 ,
11
Nocardia rugosa cobalamins, 4
Propionibacterium arabinosum cobalamins,
4
Propionibacterium freudenreichi
cobalamins, 4
Propionibacterium pentosaceum
cobalamins, 4
Propionibacterium peterssoni cobalamins,
4
Propionibacterium shermanii cobalamins,
4
Propionibacterium technicum cobalamins,
4
Protaminobacter ruber cobalamins, 4
Pseudomonas denitrificans cobalamins, 4
Rhizobium meliloti cobalamins, 4
Rhodopseudomonas spheroides
cobalamins, 4
ribose 5 - phosphate phosphoribosyltransferase, 5
Streptomyces aureofaciens cobalamins,
4
Streptomyces griseus cobalamins, 4
Strigomonas oncopelti cobalamins, 4
vitamin B 12 :
commercial production, 5
exclusive synthesis by, 4
[60Co]vitamin B 12 , 11
Microsomes, vitamin B 12 R-protein calcium
dependent transfer, 18
Migration, methylmalonyl-CoA mutase,
ethylmalonyl-CoA hydrogen,
357-379
Milk, human, cobalamin distribution,
16
Mitochondria:
cobalamins content, human liver, 16
transcobalamin, 74
vitamin B 12 R-protein calcium dependent
transfer to, 18
Model studies:
2,2-bis(aralkyloxycarbonyl)propylcholestanocobaloxime, methylmalonyl-CoA mutase, 374
2,2-bis(ethoxycarbonyl)ethylcobalamin,
methylmalonyl-CoA mutase, 374
2,2-bis(ethoxycarbonyl)propylcobaloxime
methylmalonyl-CoA mutase,
374
2-(ethoxycarbonyl)-2-(ethylthiocarbonyl)
propylcobalamin, methylmalonylCoA mutase, 374
Model systems methylmalonyl-CoA mutase,
mechanism of action, 374
Mode of rearrangement, methylmalonylCoA mutase, mechanism of action,
367
Modification:
activity diol dehydrase, vitamin B 12
coenzyme side chain, 247
diol dehydrase thiols, 242, 246
ethanolamine ammonia-lyase, 263-287
L-b-lysine mutase, 220
methylmalonyl-CoA mutase, 366
receptor binding, cobalamin propionamide
side chains, 37
ribonucleotide reductases, sulfhydryl
groups, 393
Molar extinction coefficients, see Electronic
spectrum
Molds, cobalamin occurrence, 5
Molecular properties:
diol dehydrase, 233-262
ethanolamine ammonia-lyase, 263-287
glutamate mutase:
component E, 292
component S, 292
L-leucine-2,3-aminomutase, 229
L-b-lysine mutase:
E1 component, 210
E1E2 complex, 209
E2 protein, 211
methylmalonyl-CoA mutase, 365
D-ornithine mutase Clostridia, 225
ribonucleotide reductases, 391
Molva molva, vitamin B 12 , 9
Molybdate:
acetogenic bacteria stimulation, 167
stimulation, formate dehydrogenase
production, 173
Monocarboxylic acids:
aminohexyl residue, vitamin B 12 , 38
cobalamin-binding, protein affinity,
vitamin B 12 ,60
receptor binding, vitamin B 12 , 37
tructure, vitamin B 12 , 37
Monocations, ribonucleotide reductases,
391
Monochrysis lutheri, vitamin B 12
requirement, 8
Monocyanorhodibalamin, electronic
spectrum, 131
Monocalent cations:
diol dehydrase, 241
ethanolamine ammonia-lyase, 268
L-b-lysine mutase cofactor, 218
Mucosal cells, intrinsic factor, 71
Multiple myeloma, transcobalamin, 20
Multivitamin preparations, vitamin B 12 ,
21
Mutants, cobalamins, Escherichia coli, 35
Mutant strains, cobalamins transport,
table, Escherichia coli, 35
Myelocytic leukemia:
plasma levels, cobalamins, 19
transcobalamin, 20
Myeloid leukemia, haptocorrin, 76
Myeloproliferative disease, transcobalamin,
20
Naphthimidazole corrinoids, base
incorporation, 5
2-Naphthylhydrogenobamide, cobalt
insertion, 121
Naturally occurring metal-free corrinoids,
106
Nebularylcobalamin, ribonucleotide
reductases, inhibitor constants, 401
NebularylTP, ribonucleotide reductases,
nucleotide analogs, 403
Neoplastic disease, vitamin B 12 , 19
Neuropathy therapeutic use, vitamin B 12 ,
21
Nickel enzyme:
carbon monoxide dehydrogenase, 186
Clostridium pasteuriansum, 186
Ninhydrin, L-/3-lysine mutase assay, 211
Nitrogen balance, therapeutic use,
vitamin B 12 , 22
Nitrous oxide:
bone marrow morphological changes,
comparison to vitamin B 12
deficiency, 347
inhibition, folypolyglutamate synthetase,
345
methionine synthetase, 342
ribonucleotide reductases, 410
vitamin B 128 , 346
NMR spectrum:
blue hexacarboxylic acid, 125
methylcobalamin tetrachloroplatinum(II)
complex, 157
Nocardia rugosa, cobalamins, 4
Nomenclature:
cobalamin binding proteins, 58
haptocorrin, 58
Intrinsic factor, 58
metal-free, 107
transcobalamin, 58
Noncorrinoid:
amino mutases, L-a-lysine-2,3-aminomutase, 205
5'-deoxyadenosyl radical hydrogen
carrier, 205
Non-heme iron formate dehydrogenase,
Clostridium pasteurianum, 174
Non fat dry milk, vitamin B 12 , 14
Nonintrinsic factor, see Haptocorrin
Normoblast megoblast conversion
therapeutic use, vitamin B 12 , 21
Nostoc commune, ribonucleotide reductases,
cobalamins, 384
Nucleophilic attack, methylcobalamin,
cobalt-carbon bond, 160
Nucleotide:
5.6- dimethylbenzimidazole labelled
precursors, 7
6.7- dimethyl-8-ribityllumazine labelled
precursors, 7
riboflavin labelled precursors, 7
Nucleotide analogs:
Arabino ATP, ribonucleotide reductases,
403
Arabino CTP, ribonucleotide reductases,
403
ATP ribonucleotide reductases, 403
8-bromoATP, ribonucleotide reductases,
403
N6 -dimethylATP, ribonucleotide
reductases, 403
formycin TP, ribonucleotide reductases,
403
nebularylTP, ribonucleotide reductases,
403
2’-O-methyl ATP, ribonucleotide
reductases, 403
Nucleotide analogs (Cont'd)
3 -0-methyl ATP, ribonucleotide
reductases, 403
1 -b-D-ribofuranosylbenzimidazole TP,
ribonucleotide reductases, 40 3
sangivamycin TP, ribonucleotide
reductases, 403
toyocamycin TP, ribonucleotide
reductases, 403
tubercidin TP, ribonucleotide reductases,
403
XTP (low pH), ribonucleotide reductases,
403
Xylo ATP, ribonucleotide reductases,
403
Nucleotide loop cobalamins, Escherichia
coli, 36
Nucleotide substrates, ribonucleotide
reductases, hydrogen transfer role,
405
Nutrition:
human cobalamins, 12
methionine, 340
Occurrence:
algae, vitamin B 12 , 10
archaic anaerobes, vitamin B 12 , 2
cobalamin-binding proteins biological
fluids, 60
cobalamins, 8
foodstuffs:
hydroxocobalamin, 13
methylcobalamin, 13
vitamin B 12 , 13
vitamin B 12 coenzyme, 13
a-glycosidic linkage, vitamin B 12 , 3
mammalian 5-methyltetrahydrofolate
homocysteine methyltransferase,
339
marine animals, vitamin B 12 , 2
marine environments, pseudovitamin B 12 ,
8
marine sediments, cobalamins, 8
methionine synthetase, mammalian,
339
molds, cobalamins, 5
photosynthetic bacteria, cobalamins, 4
plasma methylcobalamin, 16
before porphyrins, vitamin B 12 , 2
poultry-house litter, cobalamins, 5
rat intestines, cobalamins, 5
sea water, cobalamins, 8
yeasts, cobalamins, 5
Ochromonas danica, cobalamins, 50
Ochromonas malhamensis:
cobalamins, microbiological assay, 50,
93
growth requirement in palce of
deoxyribonucleotide, 10
methionine synthetase, 339
ribonucleotide reductases, 383
vitamin B 12 , 7
Oedogonium cardiacum, cobalamins,
50
OH-CB1, see Hydroxocobalamin
One-electron oxidation:
gold(III), methylcobalamin, 153
iridium(IV), methylcobalamin, 153
methyl radicals, methylcobalamin,
153
outer sphere, methylcobalamin, 153
One-electron reduction, methylcobalamin,
160
Oral administration, therapeutic use,
vitamin B 12 , 21
Organoborate-Iinked insoluble supports,
ribonucleotide reductases assay,
389
Origin:
granulocytes haptocorrin, 75
hepatic carcinoma cells, haptocorrin, 75
human transcobalamin, 73
life on earth, 2
red blood cells, haptocorrin, 75
saliva haptocorrin, 75
D-Ornithine amino mutases, 203-232
D-Ornithine mutase:
assay:
spectrophotometric assay, 225
thin layer chromatography, 225
catalytic properties, 226
Clostridia:
2-amino-4-ketopentanoic acid, 224
biochemical role, 224
comparison, L-/3-lysine mutase, table,
224
electronic spectrum, 225
molecular properties, 225
purification, 225
pyridoxal phosphate, 225
cofactor dithiothreitol, 226
pyridoxal phosphate, 226
vitamin B 12 coenzyme, 226
comparison to L-b-lysine mutase, table,
227
2,4-diaminovaleric acid, 206, 223
D,L-Ornithine racemase, 226
Oscillatoria prolifera, ribonucleotide
reductases, cobalamins, 384
Outer membrane cobalamins, Escherichia
coli, 35
Outer sphere:
interactions with corrin ring, cobalt-carbon
bond,156
methylcobalamin, one-electron oxidation,
153
Oxidation:
2-amino-5-ketohexanoic acid, 2,5-diaminohexanoic acid, 209
carbon monoxide enzyme, 186
hydrogenobyric acid 18,19-didehydrocobyrinic acid hexamethylester
c-amide, 125
iridium(IV) oxidation methylcobalamin,
159
methylcobalamin oxidation iridium(IV),
159
zinc corrinoids, photochemical, 128
Oxygen, diol dehydrase:
cobalt-carbon bond, 241
inactivation, 240-241
Oyster solids, vitamin B 12 , 14
Palladium(II), methylcobalamin
reaction, 155
Pancreatic protease, R-protein degradation,
18
Patterns in disease:
cobalamins, 18
transcobalamin, 19
vitamin B 12 , 18
Patterns in human, cobalamins, 12
Pentacarboxylic acid, metal-free
corrinoids, Rhodopseudomonas
capsulata, 110
Pentagastrin, intrinsic factor stimulation, 71
Pentose, ribonucleotide reductases, mechanism
mechanism of action hydrogen trans fer,
402-414
Peptidoglycan:
cobalamin transport, gram-positive
bacteria, 48
Escherichia coli cobalamins, 33, 47
Peptococcus glycinophilus:
acetogenic bacteria, 170
glycine decarboxylase, 194
Peptococcus streptococcus, acetate
biosynthesis, glycine decarboxylase, 193
Periplasma, cobalamin-binding proteins,
specificity, Escherichia coli, 38
Pernicious anemia:
cobalamin adsorption, 72
Intrinsic factor, 57
methylcobalamin concentration, 76
methylmalonyl-CoA mutase, 359
methyltetrahydrofolate acid concentra tion,
76
plasma:
cobalamin distribution, 19
methylcobalamin, 19
vitamin B 12 level, 19
reticulocyte response, 6
vitamin B 12 , 18
pH activity, ethanolamine ammonia-lyase,
267
Phenazines corrinoids, base incorporation,
5
Pehnylcupribamide, electronic spectrum,
129
Phenylhydrogenobamide:
Chromatium vinosum isolation, 107
cobalt insertion, 121
electronic spectrum, 114
Escherichia coli, growth promotion, 139
Lactobacillus Ieichmannii t growth promotion, 139
structure, 107
Phenylzincobamide, electronic spectrum,
127
Phormidium autumnale, ribonucleotide
reductases, cobalamins, 384
Phormidium luridum, ribonucleotide
reductases, cobalamins, 384
Phosphoribosyltransferase microorganisms,
ribose 5 '-phosphate, 5
Photochemical oxidation, zinc corrinoids,
128
Photolysis:
ethanolamine ammonia-lyase, 263-287
methylcobalamin, 90
methylmalonyl-CoA mutase, 366
vitamin B 12 coenzyme, 90
Phototrophs, 2
Phototropic bacteria, metal-free corrinoids,
relationship to cobalt-containing
corrinoids, 146
Physical properties:
ethanolamine ammonia-lyase, 267
methionine synthetase, 310
methylmalonyl-CoA mutase, 365
ribonucleotide reductases, 394
Physiology:
cobalamin-binding proteins, 70
diol dehydrase, 253
fundic mucosa, intrinsic factor, 71
haptocorrin, 75
intrinsic factor, 71
L-leucine-2,3-aminomutase, 228
R-protein, 18
ribonucleotide reductases, allosteric
modifiers, 398
transcobalamin, 73
Pig, vitamin B 12 requirement, 12
Pithomyces chartarum, ribonucleotide
reductases, cobalamins, 384
Pituitary, human, cobalamin distribution, 16
pKa:
methylcobalamin, base-on, base-off,
91
vitamin B 12 coenzyme, base-on, base-off,
91
Placenta, human, cobalamin analogs, 17
Placenta lactogenic hormone, intrinsic
factor, 71
Plasma:
bilirubin levels, therapeutic use,
vitamin B 12 , 21
cobalamin analogs, detection in, 17
cobalamins:
assay, 17
distribution, 16
extraction, 89
levels:
cirrhosis, 19
folic acid, 19
hepatitis, 19
myelocytic leukemia, 19
pernicious anemia, 19
concentration:
haptocorrin, 75, 89
transcobalamin, 73, 89
haptocorrin purification, 62, 64
intrinsic factor, 60
iron levels, therapeutic use, vitamin B 12 ,
21
methylcobalamin:
occurrence, 16
pernicious anemia, 19
transcobalamin, 60
vitamin B 12 :
binding proteins, 14
level, pernicious anemia, 19
role, 15
transport, 14
Platinum methylation, methylcobalamin, 157
Plectonema boryanum, ribonucleotide
reductases, cobalamins, 384
Pollack, vitamin B 12 , 9
Polycythemia vera, transcobalamin,
20
Polyploidy, 2
Pork sausage, vitamin B 12 , 14
Pork shoulder, vitamin B 12 , 14
Porphobilinogen labelled precursors,
corrin ring incorporation, 7
Potassium, therapeutic use, vitamin B 12
serum, 22
Potatoes methylmalonyl-CoA mutase,
360
Poultry-house litter, cobalamins
occurrence, 5
Practicability, cobalamins quantitation,
89
Precision, cobalamins quantitation, 89
C-1 Precursor of acetyl-CoA, carbon
monoxide, 188
Pregnancy, vitamin B 12 , 19
Preparation, Escherichia Coli 1
ethanolamine ammonia-lyase,
263-287
Priming methionine synthetase,
S-adenosyl-L-homocysteine,
347
Primitive coenzyme, vitamin B 12 coenzyme,
32
Primitive heterotrophs, 2
Principles, cobalamin isotope dilution
assays, 94
Production:
intrinsic factor, 71
molybdate stimulation formate dehydrogenase, 173
selenite stimulation formate dehydrogenase, 173
tungstate stimulation formate dehydrogenase, 173
Products from reaction methylmalonylCoA mutase ethylmalonyl-CoA
deuterated, 374
Promoters, cobalamins, Euglena gracilis, 93
( R)- 1,2-Propanediol, diol dehydrase,
substrate specificity, 239
1,2-Propanediol, diol dehydrase,
substrate specificity, 239
(S)-I,2-Propanediol, diol dehydrase,
substrate specificity, 239
1,3-Propanediol-hydroxypropionaldehyde,
diol dehy drase, gly cerol, 233-2 62
1,2-Propanediol propionaldehyde, diol
dehydrase, 233-262
Properties:
diol dehydrase:
component F, 236
component S, 236
Euglena gracilis, table, ribonucleotide
reductases, 392
Lactobacillus leichmannii, table,
ribonucleotide reductases,
392
5-methyltetrahydrofolate homocysteine
methyltransferase, mammalian,
341
Rhizobium meliloti, table, ribonucleotide
reductases, 392
Thermus X-I, table, ribonucleotide
reductases, 392
Propionaldehyde:
diol dehydrase, 1,2-propanediol,
233-262
ethanolamine a mmonia-lyase, 2 63-287
Propionamide side chain modification,
37
receptor b inding cobal amins,
Propionibacterium aeraginosa, cobalamins,
48
Propionibacterium arabinosum, cobalamins,
4
Propionibacterium freudenreichii:
cobalamins, 4
diol dehydrase, 255
Propionibacterium pentosaceum
cobalamins, 4
Propionibacterium peterssoni cobalamins,
4
Propionibacterium shermanii:
cobalamins microorganisms, 4
metabolic pathway, methylmalonyl-CoA
mutase, 359
metal-free, conversion to corrinoids,
142
methyImalonyl-CoA mutase purification,
361
Propionibacterium technicum cobalamins,
4
Propionic acid metabolism methylmalonylCoA mutase, 357-379
Propylcobalamin CD spectrum, 316
Propylcobalamin enzyme:
electronic spectrum, methionine
synthetase, 315
methionine synthetase, CD spectrum,
315
Propylcobinamide enzyme, methionine
synthetase, CD spectrum, 315
Propyl iodide inhibition, 182
homocysteine methionine biosynthesis,
323
methionine synthetase, 316, 320, 322,
336
methionine synthetase, 5-adenosyl-Lhomocysteine dependent, 336
Protaminobacter ruber cobalamins, 4
E1-Protein:
catalytic protein, L-0-lysine mutase,
209
cobamide protein, L-0-lysine mutase,
209
electronic spectrum, L-j3-lysine mutase,
210
pyridoxal phosphate, L-0-lysine mutase,
210
E2 Protein:
molecular properties, L-0-lysine mutase,
211
El protein stabilization, L-/3-lysine mutase,
214
purification, L-b-lysine mutase, 211
sulfhydryl protein, L-/3-lysine mutase, 209
R-Protein:
calcium dependent transfer microsomes,
vitamin B 12 , 18
calcium dependent transfer to mitochondria, vitamin B 12 , 18
cobalamins:
assay, 17
isotope detection, 7
degradation, pancreatic protease,
18
distribution, 18
hepatocytes, 18
physiology, 18
Sepharose affinity chromatography,
17
R-Protein binding cobalamin analogs,
18
Protein binding vitamin B 12 , 3
Protein denaturation, cobalamins
extraction, 90
Protein-histidine, aquocobalamin complex
with, 91
Proteus mirabilis, cobalamins, 48
Proton motive force, Escherichia coli y
cobalamin role, 42
Prototheca zopfi, cobalamins, 50
Prymnesium parvum, vitamin B 12 ,
exogenous nutrient, 10
Prymnesium parvum, vitamin B 12 ,
exogenous nutrient, 10
Pseudomonas aeriginosa, methionine
synthetase, 339
Pseudomonas denitrifleans, cobalamins,
4
Pseudomonas stutzeri, ribonucleotide
reductases, cobalamins, 384
Pseudovitamin B 12 occurrence, marine
environments, 8
Purification:
affinity chromatography, ribonucleotide
reductases, 387
Amberlite XAD-2, metal-free corrinoids,
108
amino terminal sequence, cobalaminbinding proteins, 62
chromatography, methylmalonyl-CoA
mutase, 362
cobalamin-binding proteins, labile-ligand
affinity chromatography, 62, 64
Cohn fraction III, cobalamin-binding
proteins, 62, 64
Cornebacterium nephridii, ribonucleotide
reductases, 388
Escherichia coliMet H mutant, 325
Euglena gracilis, ribonucleotide reductases,
388
gastric juice, intrinsic factor, 62, 64
gastric mucosa, haptocorrin, 62
glutamate mutase, 292
hog:
haptocorrin, 62, 64
intrinsic factor, 62, 64
human:
haptocorrin, 62, 64
intrinsic factor, 62, 64
transcobalamin, 62
Lactobacillus leichmannii, ribonucleotide
reductases, 386
L-leucine-2,3-aminomutase, 229
L-j3-lysine mutase:
El component, 210
E1E2 complex, 209
E2 protein, 211
5-methyltetrahydrofolate homocysteine
methyltransferase, mammalian,
341
D-ornithine mutase, Clostridia, 225
plasma haptocorrin, 62, 64
Propionibacterium shermanii, methylmalonyl-CoA mutase, 361
rabbit transcobalamin, 62
Rhizobium meliloti, ribonucleotide
reductases, 388
serum transcobalamin, 62, 64
sheep liver, methyImalonyl-CoA mutase,
360
Thermus X-I, ribonucleotide reductases,
388
Purified components, acetate biosynthesis,
188
Purine-fermenting bacteria, acetate
biosynthesis, 170
Purines:
acetate biosynthesis, 193
corrinoids, base incorporation, 5
Purinylcobamide coenzymes, Rhodospirillum
rubrum, 108
Purity:
cobalamin-binding proteins, 62
ribonucleotide reductases, 386
Pyridoxal phosphate:
L-b-lysine mutase:
E1 protein, 210
mechanism of action, 221
D-ornithine mutase:
Clostridia, 225
cofactor, 226
Pyridoxal phosphate requirement, amino
mutases, 203-232
Pyruvate:
acetate biosynthesis, 172
carboxyl group, acetic acid carboxyl group,
178
L-b-lysine mutase cofactor, 219
Pyruvate foimate-lyasQ, Escherichia coli,
181
S-adenosylmethionine cleavage, 205
Quantitation:
accuracy, cobalamins, 89
calibration standards, cobalamins, 92
clinical usefulness, cobalamins, 98
cobalamins:
haptocorrin, 98
transcobalamin bound, 98
comparison of different assay cobalamins,
97
different forms of cobalamins, 99
evaluation of method, cobalamins, 88
gastric juice, intrinsic factor, 72
human serum cobalamins, 87-104
Quantitation (Cont'd)
isotope dilution assays, cobalamin, 94
practicability, cobalamins, 89
precision, cobalamins, 89
radioimmunoassay:
intrinsic factor, 72
transcobalamin, 75
reference intervals, cobalamins, 98
specificity, cobalamins, 89
Quinazolines, corrinoids, base incorporation,
5
Rabbit:
transcobalamin purification, 62
vitamin B 12 requirement, 12
Racemase methylmalonyl-CoA mutase
methylmalonic acid, 360
Radical-carbonium ion mechanism
ribonucleotide reductases mechanism
of action, 412
Radical mechanism, ribonucleotide
reductases mechanism of action,
413
Radical pair formation:
epr spectrum, ribonucleotide reductases,
406
ribonucleotide reductases, vitamin B 12
coenzyme, 406
Radioimmunoassay:
haptocorrin, 76
intrinsic factor quantitation, 72
transcobalamin quantitation, 75
Radioisotope assay, ribonucleotide reductases
assay, 389
Radiotracer method, methionine synthetase
assay, 309
Rat, vitamin B 12 requirement, 12
Rate of cobalamin dissociation, cobalamin
receptor Escherichia coli, 38
Rat intestines, cobalamins occurrence, 5
Reaction:
with antimony(III), methylcobalamin,
155
base-on, base-off methylcobalamin, 154
with bismuth(III), methylcobalamin, 155
with chromium(II), methylcobalamin,
155
cobalamin enzymes, 3
with Iead(IV) 5 methylcobalamin, 155
with mercury(II), methylcobalamin, 154
with oxygen diol dehydrase haloenzyme,
240
with palladium(II), methylcobalamin, 155
tetramethyltin, methylcobalamin, 155
with thallium(III), methylcobalamin,
155
with tin(III), methylcobalamin, 155
Reaction pathways:
cobalt-carbon bond cleavage, 152
methylcobalamin, cobalt-carbon bond
cleavage, 152
Reactions, manganese corrinoids, 136
Reactivation, vitamin B 12 coenzyme, diol
dehydrase, 258
Rearrangement, methylmalonyl-CoA mutase:
intramolecular, 368
stereochemistry, 371
Receptor binding cobalamins:
propionamide modification, 37
vitamin B 12 monocarboxylic acids, 37
Receptor cobalamins, Escherichia coli,
cobalamin absence, 36
Reconstitution methionine synthetase
haloenzyme, 311
Red blood cells, haptocorrin origin, 75
Red tides, vitamin B 12 requirement, 8
Redox potential, cobalamins FMNH 2 ,
337
Redox-switch methylcobalamin, cobaltcarbon bond, 153, 157
Reducing systems, methionine synthetase,
catalytic, 317
Reduction:
aquocobalamin, stannous, 155
carbon dioxide, 173
manganese corrinoids, 138
ribonucleotide reductases, deoxyribonucleotide, 385
Reductive demetallation:
metal-free:
c-lactam manganese, 111
c-lactone manganese, 111
Reference intervals, cobalamins quantita tion,
98
Regimen, therapeutic use, vitamin B 12 ,
20
Regulation:
diol dehydrase apoenzyme, 257
methionine synthetase, mammalian,
339
vitamin B 12 , ribonucleotide reductases,
399
Relationship:
to cobalt-containing corrinoids,
phototropic bacteria metal-free
corrinoids, 146
Relationship (Cont'd)
to corrinoid enzyme, carbon monoxide
dehydrogenase, 189
to glycerol dehydrase, diol dehydrase,
253
Relative rates of reduction:
ATP ribonucleotide reductases, 393
CTP ribonucleotide reductases, 393
GTP ribonucleotide reductases, 393
UTP ribonucleotide reductases, 393
Relaxed radical pair:
epr spectrum, ribonucleotide reductases,
409
formation, ribonucleotide reductases,
vitamin B 12 coenzyme, 409
Release:
haptocorrin cobalamins, 75
intrinsic factor, 71
Replacement, S-adenosyl-L - methionine,
methionine synthetase methyl
iodide, 329
Requirement:
baboon, vitamin B 12 , 12
Escherichia coli, cobalamins, 33
Gymnodinium brevis, vitamin B 12 , 8
horse, vitamin B 12 , 12
human, vitamin B 12 , 13
marine fishes, vitamin B 12 , 9
marine phylo plank ton, vitamin B 12 , 8
microorganisms, cobalamins, 32
Monochrysis lutheri, vitamin B 12 , 8
pig, vitamin B 12 , 12
rabbit, vitamin B 12 , 12
rat, vitamin B 12 , 12
red tides, vitamin B 12 , 8
ruminants, vitamin B 12 , 12
sheep, vitamin B 12 , 12
Skeletonema constatum, vitamin B 12 ,
8
Resistance to free radical attack,
ethanolamine ammonia-lyase
active site, 284
Retention, vitamin B 12 coenzyme,
evolutionary, 32
Retention of configuration:
methylmalonyl-CoA mutase
stereochemistry, 372
ribonucleotide reductases, hydrogen
transfer, 403
Reticulocyte response, pernicious
anemia, 6
Reticulocytosis, therapeutic use, vitamin
B 12 , 21
Reversible cleavage, hydrogen carrier,
noncorrinoid, S-adenosylmethionine,
205
Reversible formation, ethanolamine
ammonia-lyase, 5 '-deoxyadenosine,
272, 283
Reversible methylation, vitamin B 128 ,
methionine biosynthesis,
5-methyltetrahydrofolate, 330
Rhizobia, cobalt deficient, 386
Rhizobium faponicum, ribonucleotide
reductases, cobalamins, 384
Rhizobium leguminosarum, ribonucleotide
reductases, cobalamins, 384
Rhizobium meliloti:
cobalamins, 4
methionine synthetase, 339
ribonucleotide reductases:
properties, 392
purification, 388
vitamin B 12 coenzyme, biosynthesis,
9
Rhizobium phaseoli, ribonucleotide
reductases, cobalamins, 384
Rhizobium trifolii, ribonucleotide reductases,
reductases, cobalamins, 384
Rhodibalamin, 129
Rhodibalamins, vitamin B 128 analog, 130
Rhodium analog, vitamin B 12 coenzyme,
130
Rhodium corrinoids:
axial ligand exchange, 134
electrophoretic properties, table, 135
spectral properties, 131
Rhodium corrins, electronic spectrum,
131
Rhodium insertion, metal-free
corrinoids, 128
Rhodobinamide, 129
Rhodopseudomonas capsulata, metal-free
corrinoids, 106, 110
Rhodopseudomonas palustris, metal-free
corrinoids, 106
Rhodopseudomonas spheroides:
cobalamins, 4
isolation:
hydrogenobyrinic acid a,c-diamide,
109
hydrogenobyrinic acid c-amide,
109
metal-free corrinoids, 109
yellow metal-free corrinoids, 109
methionine synthetase, 339
Rhodospirillum rubrum:
metal-free corrinoids, isolation, 6, 106,
108
methionine synthetase, 339
purinylcobamide coenzymes, 108
Riboflavin labelled precursors, nucleotide
incorporation, 7
1 -b-D-Ribofuranosylbenzimidazole TP,
ribonucleotide reductases,
nucleotide analogs, 403
Ribonucleotide analogs:
activators, ribonucleotide reductases,
402
ribonucleotide reductases, inhibition,
402
substrates, ribonucleotide reductases,
402
Ribonucleotide binding,
ribonucleotide
reductases, a llosteric modi fiers,
395
Ribonucleotide phosphate, substrate
specificity, ribonucleotide
reductases, 393
Ribonucleotide reductases:
activation:
2'-0-methyl ATP, 402
3'-0-methyl ATP, 402
activity temperature effect, 400
ADP, 2'- fluoro analog, 412
Aerobacter aerogenes, 383
allosteric modifiers:
binding sites, 395
conformation effects, 397
Cornebacterium nephridii, 398
dATP, 394
dCTP, 394
deoxyribonucleoside triphosphates,
394
dGTP, 394
dTPP, 394
Euglena gracilis, 398
fluorescence spectrum, 397
kinetic effects, 395
Lactobacillus Ieichmannii f 394
magnesium ions, 395
physiology, 398
ribonucleotide binding, 395
sedimentation binding, 397
Thermus X-I, 398
vitamin B 12r epr spectrum, 397
assay:
colorimetric assay, 390
comparison of methods, 391
fluorometric, 391
organoborate-linked insoluble supports
389
radioisotope assay, 389
spectrophotometric assay, 390
thioredoxin, 390
thioredoxin reductase, 390
tritium exchange assay, 390
ATP-Sepharose affinity, 388
biochemical role, 385
CDP, 2'-fluoro analog, 412
chemical properties, 391
2'-chloro-2'-deoxyuridine diphosphate
degradation, uracil, 412
cobalamins:
Anabaena flos-aquae, 384
Anacystis nidulans, 384
Astasia longa, 384
Bacillus megaterium KM, 384
Clostridium sticklandii, 384
Clostridium tetanomorphum, 384
Clostridium thermoaceticum, 384
Coccochloris peniocystis, 384
Corynebacterium nephridii, 384
Euglena gracilis bacillaris, 384
Euglena gracilis Z, 384
Fremyella diphlosiphon, 384
Lactobacillus acidophilus, 384
Lactobacillus leichmannii, 384
Micrococcus denitrificans, 384
Nostoc commune, 384
Oscillatoria prolifera, 384
Phormidium autumnale, 384
Phormidium luridum, 384
Pithomyces chartarum, 384
Plectonema boryanum, 384
Pseudomonas stutzeri, 384
Rhizobium japonicum, 384
Rhizobium leguminosarum, 384
Rhizobium meliloti, 384
Rhizobium phaseoli, 384
Rhizobium trifolii, 384
Scytonema hofmanni, 384
Sphaerophorus varius, 384
Synechococcus sp., 384
Thermus aquaticus, 384
Thermus X-1, 382, 384
competitive inhibitors:
aminoethylcobalamin, 401
chlorodifluoromethylcobalamin, 401
dichlorofluoromethylcobalamin,
401
formycinylcobalamin, 401
Ribonucleotide reductases (Cont'd)
methylcobalamin, 401
table, 401
conformation, temperature effect, 400
dATP-Sepharose affinity, 388
5 -deoxyadenosyl radical, epr spectrum,
408
deoxyribonucleoside binding dissociation
constants, table, 396
deoxyribonucleotide corepressor of
enzyme synthesis, 399
DNA replication, 399
reduction, 385
dGTP-Sepharose affinity, 388
4 ',5 '-didehydro-5 '-deoxyadenosine,
411
distribution:
algae, table, 383
bacteria, table, 383
of enzymes, 381418
fungi, table, 383
disulfide bridges, 393
dithiols,414
DNA replication:
allosteric modifier, 399
dNTP formation, 399
DNA synthesis:
allosteric modifiers, 399
dNTP's relative amounts, 399
effect of ions, 391
electron transport, 385
epr, vitamin B 12 coenzyme degradation,
406
Escherichia coli, 383
glutathione, glutathione reductase, 386
hydrogen donors:
dihydrolipoate, 386
dithioerythritol, 386
dithiothreitol, 386
hydrogen exchange, dithiols, 404
hydrogen transfer:
retention of configuration, 403
role, nucleotide substrates, 405
sterochemistry, 403
to and from w ater, 402 , 404
, 409
hydroxyl group migration
inhibition:
arabino ATP, 402
FTP, 402
methoxybenzimidazolylcobamide,
401
2-methyladen-9-ylcobamide, 401
ribonucleotide analogs, 401
inhibitor constants, 401
inhibitors:
cobalamins, table, 401
vitamin B 12 coenzyme analogs, 400
kinetic behavior, 391
Lactobacillus leichmannii, 382
mechanism of action:
cobalt-carbon bond cleavage, 410
hydrogen transfer pentose, 402
ionic mechanism, 411
mercaptocobalamin, 412
radical-carbonium ion mechanism, 412
radical mechanism, 413
role dithiol, 412
vitamin B 128 , 410
mechanistic schemes dithiols, 409
Methanobacillus omelianskii, 383
modification, 393
molecular properties, 391
monocations, 391
nitrous oxide, 410
nucleotide analogs, 404
Ochromonas malhamensis, 383
physical properties, 394
properties:
Euglena gracilis, table, 392
Lactobacillus leichmannii, table, 392
Rhizobium meliloti, table, 392
Thermus X-I, table, 392
purification:
affinity chromatography, 387
Cornebacterium nephridii, 388
Euglena gracilis, 388
Lactobacillus leichmannii, 386
Rhizobium meliloti, 388
Thermus X-I, 388
purity, 386
radical pair formation, epr spectrum,
406
relative rates of reduction:
ATP, 393
CTP, 393
GTP, 393
UTP, 393
relaxed radical pair, epr spectrum, 409
Rhizobium meliloti, 9
ribonucleotide analogs:
activators, 402
substrates, 402
ribonucleotide phosphate, substrate
specificity, 393
substrate specificity, 393
sulfhydryl groups, modification, 393
Ribonucleotide reductases (Cont'd)
thiols, 393
thioredoxin:
fluorescence spectrum, 385
thioredoxin reductase, 385
VitaminB 12 coenzyme:
analog binding, 400
analogs as coenzymes, 400
analogs as inhibitors, 400
binding, 395
cobalt-carbon bond cleavage, 408,
410
degradation, epr spectrum, 406
hydrogen exchange with water, 404
radical pair formation, 406
relaxed radical pair formation, 409
Sepharose affinity, 388
[5 '-3H] -vitamin B 12 coenzyme assay,
390
see also Hydrogen exchange; Hydrogen
transfer
[14C] Ribonucleotides DNA incorporation,
cobalamin dependence, Lactobacillus
leichmannii, 383
Ribose 5 '- phosphate phosphoribosyltransferase microorganisms, 5
Role:
dithiol ribonucleotide reductases,
mechanism of action, 412
human L-leucine-2,3-aminomutase, 228
metal-free corrinoids, vitamin B 12
biosynthesis, 143
methionine synthetase, S-adenosyl-Lmethionine, 329
nucleotide substrates, ribonucleotide
reductases, hydrogen transfer, 405
plasma vitamin B 12 , 15
proton motive force, Escherichia coli
cobalamins, 42
tetrahydrofolic acids, acetate biosynthesis, 174
Ton B gene product, Escherichia coli
cobalamins, 42
transcobalamin I, 14
transcobalamin II, 14
Ruminants, vitamin B 12 requirement,
12
Ruminococcus flavefaciens, vitamin B 12
exogenous nutrient, 10
formyl-methylSaccharomyces C
erevisiae t
methylenetetrahydrofolate sy
nthetase, 176
Saliva:
binder protein, 58
cobalamins, isotope dilution assays,
95
haptocorrin origin, 60, 71, 75
Salmonella paratyphi, cobalamins, 48
Salmonella typhimurium:
cobalamins, 48
ethanolamine ammonia-lyase, 263-287
Met H mutant, methionine synthetase,
322
methionine synthetase, 339
Sangivamycin TP, ribonucleotide
reductases, nucleotide analogs,
403
Schiff-base intermediate L-/3-lysine mutase,
mechanism of action, 221
Schilling I and II tests, 72
Scopulariopsis brevicaulis, Gossio's gas
trimethylarsine, 151
Scytonema hofmanni, ribonucleotide
reductases, cobalamins, 384
SDS polyacrylamide:
cobalamin-binding protiens, 65
cobalamins, occurrence in, 8
Sedimentation binding, ribonucleotide
reductases, allosteric modifiers, 397
Selenite:
acetogenic ba cteria stimula tion, 167
stimulation, formate dehydrogenase
production, 173
Separation:
coated charcoal, cobalamins, 96
free and protein bound cobalamins, 96
haptocorrin, transcobalamin, 75
insolubilized binding protein, cobalamins,
97
metal-free corrinoids, Rhodopseudomonas
capsulata, 111
Sepharose affinity chromatography:
cobalamin-binding proteins, 60
R-protein, 17
ribonucleotide reductases, vitamin B 12
coenzyme, 388
Serratia marCescens y vitamin B 12 exogenous
nutrient, 11
Serum:
alkaline phosphatase, therapeutic use,
vitamin B 12 ,22
cobalamins:
extraction, 89
present, 88
quantitation, human, 87-104
Serum (Cont'd)
concentration cobalamins, 89
folic acid, therapeutic use, vitamin B 12 ,
22A
potassium, therapeutic use, vitamin B 12 ,
22
transcobalamin purification, 62, 64
Sewage sludge, dietary supplement,
Epystylis, 6
Sheep:
cobalt, 12
livery methylmalonyl-CoA mutase
purification, 360
vitamin B 12 requirement, 12
Sialic acid content:
haptocorrin, 76
intrinsic factor decreased production, 71
transcobalamin, 20
Side chain:
a-(lower)-ligand modification activity,
diol dehydrase, vitamin B 12 coenzyme, 248
b-(upper) -Iigand modification activity,
diol dehydrase, vitamin B 12 coenzyme, 249
modification activity, diol dehydrase,
vitamin B 12 coenzyme, 247
Size change, cobalamin binding, intrinsic
factor, 71
Skeletonema costatum, vitamin B 12
requirement, 8
Somatostatine, intrinsic factor, decreased
production, 71
Source:
cobalamin analogs, 18
methylmalonyl-CoA mutase, 357-379
in nature, table, cobalamins, 3
vitamin B 12 coprophagy, 12
Specific activity, methionine synthetase,
311
Specificity:
cobalamins, quantitation, 89
Escherichia coli periplasma, cobalaminbinding proteins, 38
aIower)-Iigand modification activity,
table, glutamate mutase vitamin B 12
coenzyme, 294
Spectral properties, see Electronic spectrum
Spectrophotometric assay:
L-b-lysine mutase assay, 211
methylmalonyl-CoA mutase assay, 364
D-ornithine mutase assay, 225
ribonucleotide reductases assay, 390
Sphaerophoms Varius y ribonucleotide
reductases, cobalamins, 384
Spleen, human, cobalamin distribution,
16
Standard curves, cobalamin isotope dilution assays, theoretical, 94
Stannous reduction, aquocobalamin,
155
Stereochemistry;
2-aminopropanol ethanolamine ammonialyase, 263-287
deamination, ethanolamine ammonialyase, 263-287
hydrogen transfer, diol dehydrase, 243
hydroxyl group transfer, diol dehydrase,
242
rearrangement, methylmalonyl-CoA
mutase, 371
retention of configuration, methylmalonylCoA mutase, 372
ribonucleotide reductases, hydrogen
transfer, 403
Stereospecificity, methionine synthetase,
methyl group transfer, 318
Stimulation:
appetite vitamin B 12 , therapeutic use,
21
ferrous sulfate, acetogenic bacteria, 167
folic acid, acetogenic bacteria, 167
formate dehydrogenase production:
molybdate, 173
selenite, 173
tungstate, 173
histamine, intrinsic factor, 71
insulin, intrinsic factor, 71
molybdate, acetogenic bacteria, 167
pentagastrin, intrinsic factor, 71
selenite, acetogenic bacteria, 167
therapeutic use, vitamin B 12 growth,
21
vitamin B 12 acetogenic bacteria, 167
Stokes radii:
cobalamin-binding proteins, 67
intrinsic factor, acceptor-cobalamin
complex, 72
methionine synthetase, 314
transcobalamin acceptor, 74
Streptomyces aureofaciens, cobalamins,
microorganisms, 4
Streptomyces griseus, cobalamins, 4
Streptomyces olivaceus:
metal-free corrinoids, 6, 107
methionine synthetase, 339
Strigomonas on copelti, cobalamins, 4
Structure:
(2S)-alaninol, 372
a-benzimidazolyhydrogenobamide,
111
2,2-bis(aralkyloxycarbonyl)propylcholestanocobaloxime, 375
5,15 -bisdesmethylhy drogenoby rinic
acid hexamethyl ester c-dimethylamide, 113
2,2-bis(ethoxycarbonyl)ethylcobalamin,
375
2,2-bis(ethoxycarbonyl)propylcobalamin,
375
2,2-bis(ethoxycarbonyl)propylcobaloxime,
375
bridged cobaloxime, 375
capped cobaloxime, 375
cobalamin-binding proteins, 63
cobyrinic hexamethylester c-lactone, 121
15 -cyano-1,2,2,7,7,12,12-heptamethylcorrin, 113
1 8-dehydro-l 7-desmethylhydrogenocobyrinic acid, 145
18,19-didehydrocobyrinic acid hexamethylester c-amide, 126
18,19-didehydrogenobyrinic acid, 145
diol dehydrase subunit, 237-238
ethanolamine ammonia-lyase, 263-287
2-(ethoxycarbonyl)-2-(ethylthiocarbonyl) propylcobalamin, 375
ethylmalonyI-CoA deuterated stereospecifically, 373
5-hydro-6-amino-dehydrogenobyrinic
acid a-amide c-lactam, 120
hydrogenobalamin, 107
hydrogenobamide, 107
hydrogenobinamide, 107
hydrogenobyric acid, 107
hydrogenobyric acid a -lactam, 112
hydrogenobyric acid c-lactone, 112
hydrogenobyrinic acid, 107
hydrogenobyrinic acid a, c-diamide, 120
( -)-3-hydroxyisobutanoic acid, 371
(25, 3,S)-3-methylaspartic acid, 372
methylmalonyl-CoA, 372
phenylhydrogenobamide, 107
vitamin B 12 monocarboxylic acids, 37
Substrates:
kinetic constants, ethanolamine ammonialyase, 263-287
ribonucleotide reductases, ribonucleo tide
analogs, 402
Substrate specificity:
dioldehydrase, 239
glycerol, diol dehydrase, 239
isobutylene glycol, raeso-2,3-butanediol,
diol dehydrase, 239
methionine synthetase, methyl group
transfer, 318
ribonucleotide reductases, ribonucleotide
phosphate, 393
L-b-lysine mutase, 220
Subunit:
dissociation, diol dehydrase, 236
ethanolamine ammonia-lyase, 263-287
structure, diol dehydrase, 237-238
vitamin B 12 coenzyme binding, glutamate
mutase, 296
(+)-(2S)-[2-2HI] -Succinic acid, 372
Succinyl-CoA methylmalonyl-CoA mutase,
357-379
Sulfhydryl groups:
ethanolamine ammonia-lyase, 263-287
glutamate mutase, component S, 293
glycerol dehydrase, 254
methylmalonyl-CoA mutase, 366
L-b-lysine mutase, 221
methylmalonyl-CoA mutase, 366
modification, ribonucleotide reductases,
393
Sulfhydryl protein, L-j3-lysine mutase,
E2 protein, 209
Sulfitocobalamin, methionine synthetase,
haloenzyme reconstitution, 88, 313
Sulfur metabolism, mammalian, 340
Swiss cheese, vitamin B 12 , 14
Synechococcus sp., ribonucleotide
reductases, cobalamins, 384
Synthesis:
15-cyano-l,2,2,7,7,12,12-heptamethylcorrin, 112
microorganisms cobalamins, 4
transcobalamin:
fibroblasts, 73
macrophage, 73
unidentified microorganisms, cobalamins, 6
Synthetic metal-free corrins, 112
TC(II), sec R-Protein
TCI, see Transcobalamin I
TCIII, see Transcobalamin III
Temperature effect, ribonucleotide
reductases:
activity, 400
conformation, 400
Terminal galactose residue, haptocorrin,
76
Tetracarboxylic acid metal-free
corrinoids, Rhodopseudomonas
capsulata, 110
Tetrachloropalladium(II) complex,
methylcobalamin, 157
Tetrachloroplatinum(II) complex, NMR
spectrum, methylcobalamin, 157
Tetraethyllead toxicity, 154
Tetrahydrofolate enzymes:
Acetobacterium woodii, 176
Clostridium formicoaceticum, 176
Clostridium thermoaceticum, 176
Escherichia coli, 176
homoacetate-fermenting bacteria, 168
levels in corrinoid pathway, 175
Tetrahydrofohc acid, acetate biosynthesis
role, 174
Tetramethyltin, methylcobalamin reaction,
155
Tetranitromethane inactivation,
L-/3-lysine mutase, 221
Thallium(III), methylcobalamin
reaction, 155
Theoretical standard curves, cobalamin
isotope dilution assays, 94
Theoretical studies, methylmalonyl-CoA
mutase, mechanism of action,
376
Therapeutic use:
cobalamin, 20
hydroxocobalamin, 20
methylmalonic aciduria, vitamin B 12 ,
21
vitamin B 12 :
administration, 20
allergies, 21
appetite stimulant, 21
bone marrow aspirate, 21
clinical response, 21
dermatologic disorders, 21
dose, 20
erythropoiesis, 22
folic acid, 22
growth stimulation, 21
hemoglobin levels, 22
hypochromia, 22
liver disease, 21
megoblast to normoblast conversion,
21
neuropathy, 21
nitrogen balance, 22
oral administration, 21
plasma:
bilirubin levels, 21
iron levels, 21
lactic dehydrogenase, 21
regimen, 20
reticulocytosis, 21
serum:
alkaline phosphatase, 22
folic acid, 22
potassium, 22
uric acid, 22
urine phosphorus, 20, 22
Therapy, see Therapeutic use
Thermus aquaticus:
ribonucleotide reductases, cobalamins,
384
vitamin B 12 exogenous nutrient, 11
Thermus X-I, ribonucleotide reductases:
allosteric modifiers, 398
cobalamins, 384
properties, 392
purification, 388
Thin layer chromatography:
L-0-lysine mutase assay, 213
D-ornithine mutase assay, 226
Thioglycerol diol dehydrase substrate
specificity, 239
Thiols:
diol dehydrase, active site, 241
methylation, methylcobalamin, 156
modification, diol dehydrase, 246
Thioredoxin:
fluorescence spectrum, ribonucleotide
reductases, 385
ribonucleotide reductases, 393
ribonucleotide reductases assay, 390
thioredoxin reductase, ribonucleotide
reductases, 385
Thioredoxin reductase, ribonucleotide
reductases assay, 390
thioredoxin, 385
Threonine labelled precursors, l-amino-2propanol, 7
Thymidylcobalamin, ribonucleotide
reductases, inhibitor constants,
401
Tin(III), methylcobalamin reaction with,
155
Tin biomethy
lation, 161
Tin iodide
toxicity, 154
Tissue:
cobalamin analogs distribution, 17
Tissue (Cont'd)
cobalamins assay, 16
hydroxocobalamin, 15
methionine biosynthesis, mammalian,
307-355
methyl cobalamin, 15
vitamin B 12 ,15
vitamin B 12 binding methionine
synthetase, mammalian, 339
vitamin B 12 coenzyme, 15
Toad fish binder protein cobalamins, isotope
dilution assay, 95
To and from water, ribonucleotide
reductases, hydrogen transfer,
402, 404
Ton B gene product:
cobalamins:
Escherichia coli, 43
transport, 43
Escherichia coli cobalamins role, 42
ferric:
enterochelin, 43
ferrichrome, 43
Iron chelate transport bacteriophage Tl,
42
Toxicity:
lead acetate, 154
mercuric chloride, 154
methylmercurie chloride, 154
tetraethyllead, 154
tin iodide, 154
trimethyltin acetate, 154
Toyocamycin TP, ribonucleotide reductases,
nucleotide analogs, 403
Transalkylation mechanism, glycylcobalamin,
ethanolamine ammonia-lyase, 263- 287
Transcarboxylation:
acetate biosynthesis, 173
acetic acid carboxyl group, 178
Transcobalamin:
acceptors calcium, 74
alleles, 73
amino acid composition, 63, 67
amino terminal sequence, 66
amino terminal, 69
antibody, 75
autoimmune disease, 20
carbohydrate composition, 63, 67, 73
cobalamins:
aquocobalamin complex with, 70
conformational change, 74
isotope dilution assays, 95
congenital lack, 74
defects, 73
degradation, 74
electronic spectrum:
hydroxocobalamin complexed with,
70
vitamin B 12 complexed with, 66,
70
fibroblasts synthesis, 73
gastrointestinal carcinoma, 20
Gaucher's disease, 20
half-life, 74
hepatoma, 20
IgG complex, 20
ileal synthesis, 73
immunology, 70
infectious leukocytosis, 20
isoproteins, 73
leukocyte count, comparison to, 20
liver as source, 73
macrophage synthesis, 73
metastatic breast carcinoma, 20
mitochondria uptake, 74
multiple myeloma, 20
myelocytic leukemia, 20
myeloproliferative disease, 20
nomenclature, 58
origin human, 73
patterns in disease, 19
physiology, 73
plasma concentrations, 60, 73, 89
polycythemia vera, 20
purification:
human, 62
abbit, 62
serum, 62, 64
quantitation radioimmunoassay, 75
eparation haptocorrin, 75
s ialic acid content, 20, 57-85
see also Cobalamin binding proteins,
receptors, transport
Transcobalamin acceptor, Stokes radii,
74
Transcobalamin bound cobalamins,
quantitation, 98
Transcobalamin I:
binding capacity, 15
half-life, 15
role, 15
Transcobalamin II:
binding capacity, 15
half-life, 15
role, 15
Transcobalamin III, 14
Transcorrin II, see Transcobalamin
Transmethylase:
acetate biosynthesis, 173
"corrinoid" enzyme, 183
Transmethylation corrinoids, methyltetrahydrofolate, 176
Transport:
Escherichia coli:
cobalamins, 33, 43
mutant strains, cobalamins, 35
microorganisms, cobalamins, 31
plasma vitamin B 12 , 14
Ton B gene product cobalamins, 43
Tricarboxylic acid, metal-free corrinoids,
Rhodopseudomonas capsulata,
110
Trifluoropropanediol, diol dehydrase,
substrate specificity, 239
Trimethylarsine:
biosynthesis, Gossio's gas, 152
Scopulariopsis brevicaulis, Gossio's gas,
152
Trimethyltin, acetate toxicity, 154
Triphosphates, ribonucleotide reductases,
allosteric modifiers, deoxyribonucleoside, 394
Tritium exchange assay, ribonucleotide
reductases, 390
Tubercidin TP, ribonucleotide reductases,
nucleotide analogs,403
Tuna (canned
), v
itamin B
12 , 14
Tungstate stimulation, formate dehydrogenase
production, 173
Undetected by microbiological assay
cobalamins, 17
Unidentified microorganisms, cobalamins
synthesis, 6
Unknown function:
Clostridium formicoaceticum, corrinoid
proteins, 190
Clostridium thermoaceticum, corrinoid
proteins, 190
Uptake Escherichia coli, vitamin B 12 , 34
Uracil, ribonucleotide reductases,
2'- chloro-2 '-deoxyuridine
diphosphate degradation, 412
Uric acid:
acetate biosynthesis, 170
therapeutic use, vitamin B 12 , 22
Uridylcobalamin, ribonucleotide reductases,
Inhibitor constants, 401
Urine phosphorus, therapeutic use,
vitamin B 12 , 22
Use of cyanide, cobalamin extraction, 91
UTP:
deoxynucleoside triphosphate binding,
ribonucleotide reductase, 396
ribonucleotide reductases, relative rates
of reduction, 393
UV spectra, see Electronic spectrum
Visible spectra, see Electronic spectrum
Vitamin B 12 :
acetogenic bacteria stimulation, 167
administration, therapeutic use, 20
alfalfa, 9
allergies, therapeutic use, 21
Anabena cylindria, 9
appetite stimulant, therapeutic use,
21
aquocobalamin conversion, 91
binding methionine synthetase, mammalian
tissue, 339
beef, 14
binding intrinsic factor:
metal-free inhibition, 141
VitaminB 12 inhibition, 141
binding proteins plasma, 14
bioautography, 7
biosynthesis:
cobalt incorporation, 144
role, metal-free corrinoids, 143
biosynthetic precursor:
18-dehydro-17-desmethylhydrogenobyrinic acid, 145
metal-free corrinoids, 145
bone marrow aspirate, therapeutic use, 21
buttermilk, 14
Camembert cheese, 14
chicken breast, 14
chicken liver, 14
Chlorella vulgaris, 9
clam solids, 14
clinical response, therapeutic use, 21
cobalt removal, 106
commercial production, microorganisms,
5
complexed:
with haptocorrin, electronic spectrum,
66,70
with intrinsic factor, electronic
spectrum, 66, 70
with transcobalamin, electronic
spectrum, 66, 70
Vitamin B 12 (Cont'd)
coprophagy source, 12
cottage cheese, 14
Danish depot preparation, 20
deficiency, 5-methyltetrahydrofolate
megoblastic anemia, 18, 344
dependent methyl transfer, 151-164
dermatologic disorders, therapeutic
use, 21
distribution:
human, 16
in nature, 6,19
dose, therapeutic use, 20
egg white, 14
egg yolk, 14
erythropoiesis, therapeutic use, 22
Escherichia coli strains, 7, 11
Euglena gracilis, 1
evolutionary antiquity, 1
exclusive synthesis by microorganisms,
4
exogenous nutrient:
Arthrobacter sp. (No. 38), 10
Azobacter vinelandii, 11
Bacillus megaterium, 11
Prymnesium parvum, 10
Ruminococcus flavefaciens, 10
Serratia marcescens, 11
Thermus aquaticus, 11
Facus, 9
flounder, 14
folic acid, therapeutic use, 22
Gadus pollackius, 9
growth stimulation, therapeutic use,
21
ham, cured, 14
hemoglobin levels, therapeutic use,
22
human absorption, 13
hypochromia, therapeutic use, 22
ileal disease, 19
inhibition, vitamin B 12 binding, intrinsic
factor, 141
Lactobacillus Ieichmannii y 7
lamb kidney, 14
lamb liver, 14
lamb stew meat, 14
Laminaria 1 9
level, pernicious anemia plasma, 19
ling, 9
liver disease, therapeutic use, 21
lobster, 14
marine species, 8
Medicago, 9
megoblast to normoblast conversion,
therapeutic use, 21
metal analogs:
antimetabolite properties, 139
bone marrow, 141
cobalamin-binding proteins, 140
microbial growth promotion, 139
methionine biosynthesis, 307-355
methionine synthetase, haloenzyme
reconstitution, 313
methylmalonic aciduria, therapeutic use,
20
microbiological assay, 7
microorganisms:
assay, 7
classification, 10
Escherichia coli, 11
Lactobacillus leichmannii, 11
[60Co] vitamin B 12 , 11
Molva molva, 9
monocarboxylic acid, cobalamin-binding
proteins, affinity, 60
monocarboxylic acids:
aminohexyl residue, 38
receptor binding, 37
structure, 37
multivitamin preparations, 21
neoplastic disease, 19
neuropathy, therapeutic use, 21
nitrogen balance, therapeutic use, 22
nonfat dry milk, 14
occurrence:
algae, 10
archaic anaerobes, 2
foodstuffs, 13
a-glycosidic linkage, 3, 8-10
marine animals, 2
before porphyrins, 2
Ochromonas malhamensis, 1
oral administration, therapeutic use,
21
oyster solids, 14
patterns in disease, 18
pernicious anemia, 18
plasma:
bilirubin levels, therapeutic use, 21
iron levels, therapeutic use, 21
lactic dehydrogenase, therapeutic
use, 21
pollack, 9
pork sausage, 14
pork shoulder, 14
Vitamin B 12 (Cont'd)
pregnancy,19
protein binding, 3
R-protein:
calcium dependent transfer microsomes,
18
calcium dependent transfer to
mitochondria, 18
regimen, therapeutic use, 20
requirement:
baboon,12
Gymnodinium brevis, 8
horse, 12
humans, 12, 13
marine fishes, 9
marine phyloplankton, 8
Monochrysis lutheri, 8
Pig, 12
rabbit, 12
rat, 12
red tides, 8
ruminants, 12
sheep, 12
Skeletonema costatum, 8
reticulocytosis, therapeutic use, 21
ribonucleotide reductases, regulation,
399
role plasma, 15
serum:
alkaline phosphatase, therapeutic use,
22
folic acid , therap eutic use , 22
potassium, therapeutic use, 22
sheep, 12
Swiss cheese, 14
tissue, 15
transport plasma, 14
tuna (canned), 14
UptsikQ i Escherichia coli, 34
uric acid, therapeutic use, 22
urine phosphorus, therapeutic use, 22
whole pasteurized milk, 14
yoghurt, 14
see also Cobalamins; Corrinoids;
Corrins; VitaminB 12 coenzyme
Vitamin B 12r :
enzyme, methionine biosynthesis,
337
epr spectrum, ribonucleotide reductases,
allosteric modifiers, 397
ethanolamine ammonia-lyase, 274
methionine, synthetase, haloenzyme
reconstitution, 313
VitaminB 12 coenzyme degradation,
406
Vitamin B 12s :
analog, rhodibalamin s, 130
electronic spectrum, methionine
synthetase, 334
enzyme, methionine synthetase, 330, 333
ethanolamine ammonia-lyase, 263-287
iron analog, 138
methionine synthetase, 330
nitrous oxide reaction, 346
ribonucleotide reductases, mechanism
of action, 410
VitaminB 12 coenzyme:
S-adenosylmethionine as replacement,
206
L-2-aminopropanol, ethanolamine
ammonia-lyase, 263-287
anaerobic organisms, 32
analogs:
binding, ribonucleotide reductases, 400
as coenzymes, ribonucleotide
reductases, 400
as cofactors, ethanolamine ammonialyase, 267
as inhibitors, ribonucleotide reductases,
400
methylmalonyl-CoA mutase, 366
ribonucleotide reductase, inhibitors,
400
assay, ribonucleotide reductases, 390
base-on, base-off pKa, 91
binding:
ethanolamine ammonia-lyase, 263-287
glutamate mutase subunit, 298
ribonucleotide reductases, 395
biosynthesis Rhizobium meliloti, 9
cobalt-carbon bond:
activation, diol dehydrase, 251
cleavage, ethanolamine ammonialyase, 263-287
cobalt-carbon bond cleavage, ribonucleotide reductases, 408, 410
60
Co-Iabelled, 92
complexed with platinum salts, 161
degradation:
5 '-deoxyadenosine, 406
epr spectrum, ribonucleotide reductases,
406
ribonucleotide reductases, epr, 406
vitamin B 12r , 406
Vitamin B 12 coenzyme (Cont'd)
5 -deoxyadenosyl radical, ethanolamine
tissue, 15
Vitamins, evolutionary appearance, 2
ammonia-lyase, 263-287
diol dehydrase reactivation, 257
Water, ribonucleotide reductases,
hydrogen transfer to and from,
402, 404
distribution, human, 16
Escherichia coli cobinamide to, 5
ethanolamine ammonia-lyase:
isotope effects, 263-287
Whole pasteurized milk, vitamin B 12 ,
14
mechanism of action, 263-287
evolutionary retention, 32
Xanthine, acetate biosynthesis, 170
haptocorrin bound conversion aquo-
X-ray crystallography, 5-hydro-6-amino-
cobalamin, 90
hydrogen carrier:
ethanolamine ammonia-lyase, 263-287
isotope effects, 223
L-0-lysine mutase, 222
hydrogen exchange with water, ribonucleotide reductases, 404
hydrogen migration, methylmalonyl-CoA
mutase, 368
dihydrocobyrinic acid pentamethylester a-mide c-lactam, 124
X-ray structure:
byrinic acid a, c-diamide, 132
15-cy ano -1,2,2,7,7,12,12-heptamethylcorrin, 112
dicyanorhodibyrinic acid fl,c-diamide,
132
XTP (low pH), ribonucleotide reductases,
nucleotide analogs, 403
hydrogen transfer, diol dehydrase, 243
inhibitors, methy lmalonyl-CoA mutase, 366
isotope effects, methylmalonyI-CoA
mutase, 369
L-b-lysine mutase cofactor, 207, 217
methionine synthetase, haloenzyme
Yeasts cobalamins occurrence, 5
Yellow cobalt containing corrinoids, to
red form, electronic spectrum, 124
Yellow conversion products, metal-free,
reconstitution, 313
methylmalonyl-CoA mutase, 357-379
123
Yellow corrinoids, zinc corrinoids,
occurrence foodstuffs, 13
D-ornithine mutase cofactor, 226
conversion to, 128
Yellow hydrogenobyric acid base
photolysis, 90
primative coenzyme, 32
titration, electronic spectrum, 119
Yellow metal-free corrinoids, Rhodopseudomonas spheroides isolation,
radical pair formation, ribonucleotide
reductases, 406
relaxed radical pair formation, ribonu-
109
Yellow product I, metal-free corrinoids,
cleotide reductases, 409
rhodium analog, 130
114
Yellow product II, metal-free corrinoids,
Sepharose affinity, ribonucleotide
reductases, 388
115
Yoghurt, vitamin B 12 ,14
side chain:
a-(lower)-ligand modification activity,
diol dehydrase, 248
Zinc corrinoids:
conversion to yellow corrinoids, 128
b-(upper)-Iigand modification activity,
photochemical oxidation, 128
diol dehydrase, 249
Zinc incorporation, metal-free corrinoids,
modification activity, diol dehydrase,
126
247
Zincobalamin, electrophoretic mobilities,
specificity, a-(lower)-Iigand modifica tion
activity, table, glutamate
mutase, 294
127
Zincobyric acid, electronic spectrum,
126