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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. 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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. 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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. 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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. 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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. 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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. 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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. 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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. 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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. 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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