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Chapter Five - DORAS
Chapter Five - DORAS

... The purification of membrane proteins from total membrane fractions can be facilitated by the use of affinity tags and immobilised metal ion affinity chromatography (IMAC) techniques. In silico analysis was required to establish the predicted size, location and topology of the membrane proteins prio ...
Identification of possible tworeactant sources of
Identification of possible tworeactant sources of

... described in 1938 [l] and have since then been the subject of extensive studies. Several attempts have been made to trace the mechanical origin of the oscillations [2 - 101. Such attempts have usually been based on intuitive reasoning and concerned possible oscillatory sources tentatively selected b ...
Neurodegeneration from Mitochondrial Insufficiency
Neurodegeneration from Mitochondrial Insufficiency

... The capability of their mitochondria to produce large quantities of ATP from the diet likely empowered the early single-celled eukaryotes to evolve within cellular communities as sophisticated as those of the human body. But with this advance came a challenge: the erosive effects of the highly react ...
Human Physiology - Coastline Community College
Human Physiology - Coastline Community College

... In absence of O2, NADH gives its Hs to pyruvate creating Lactic acid (Anaerobic Respiration) In ...
Biochemistry: A Short Course
Biochemistry: A Short Course

... methylmalonyl CoA mutase, a vitamin B12 requiring enzyme. ...


... Choice B: A protein has a native molecular weight of 180 kDa. SDS-PAGE obtained in the presence of β-mercatoethanol (BME) shows three bands of equal intensity, with molecular weight of 10 (αchain), 30(β-chain), and 50(γ-chain) kDa. i) What technique was used to determine the native molecular weight? ...
exam2_2011_key
exam2_2011_key

... Choice B: A protein has a native molecular weight of 180 kDa. SDS-PAGE obtained in the presence of -mercatoethanol (BME) shows three bands of equal intensity, with molecular weight of 10 (chain), 30(-chain), and 50(γ-chain) kDa. i) What technique was used to determine the native molecular weight? ...
Studies Into the Allosteric Regulation of ADP
Studies Into the Allosteric Regulation of ADP

... reasons, there has been extensive research into understanding the metabolic pathways involved with glycogen and starch synthesis. Structurally, these polysaccharides take the form of glycogen in bacteria, and starch ...
Enzyme Mechanisms - Illinois Institute of Technology
Enzyme Mechanisms - Illinois Institute of Technology

... Enzyme usually works on esters too Found in eukaryotic digestive enzymes and in bacterial systems Widely-varying substrate specificities ...
Saimaa University of Applied Sciences Faculty of Technology, Imatra, Finland ’s Degree Bachelor
Saimaa University of Applied Sciences Faculty of Technology, Imatra, Finland ’s Degree Bachelor

... Enzymes, as industrial biocatalysts, are a class of proteins extracted from animals, plants, and microorganisms. It has a board range of applications in different industries such as food, textiles, pharmaceuticals, detergents, paper and pulp, waste management, etc. Modern enzyme industry is high-tec ...
Energy Substrate Metabolism in - Journal of Clinical Investigation
Energy Substrate Metabolism in - Journal of Clinical Investigation

... in 24 hr and 7.5% in 48 hr. By comparison with the much greater per cent decreases in the rates of oleic acid-1-'C oxidation after storage of the platelets, the small changes in specific radioactivity of the fatty acid pool were considered negligible. Changes in the specific activity of the fatty ac ...
Autotrophic carbon fixation in archaea
Autotrophic carbon fixation in archaea

... the transduction of H+ or Na+ across the cytoplasmic membrane, and the archaeal H+ ATP synthase uses the resultant proton-motive force for ATP synthesis. Reducing power for biosynthesis is also provided by the oxidation of reduced inorganic substrates, although ...
Autotrophic carbon fixation in archaea
Autotrophic carbon fixation in archaea

... the transduction of H+ or Na+ across the cytoplasmic membrane, and the archaeal H+ ATP synthase uses the resultant proton-motive force for ATP synthesis. Reducing power for biosynthesis is also provided by the oxidation of reduced inorganic substrates, although ...
The Role of Nucleoside Diphosphate Kinase in Plant Mitochondria
The Role of Nucleoside Diphosphate Kinase in Plant Mitochondria

... organisms from bacteria to human. It was discovered that the genes nm23 and awd, which encode NDPKs are involved in tumour metastasis and Drosophila development, respectively. Thus, NDPK isoforms have been suggested to have specific regulatory functions in addition to their catalytic activity. Plant ...
Presence of Anaplerotic Reactions and Transamination, and the
Presence of Anaplerotic Reactions and Transamination, and the

... observations that the same strain had cytochrome pigments and evidence for the presence of oxidative phosphorylation activity (VanDemark & Smith, 1964a). However, the relationship was diminished by our contrary finding that cytochrome pigments are absent from the 07 strain and from other Mollicutes ...
PDF - Oxford Academic
PDF - Oxford Academic

... these conditions, the organisms contain less than 10% the normal amount of phycocyanin, a photopigment which accounts for up to 20% of the protein of phototrophic cells. This reduction in a major protein species could, in part, account for the increased specific activities observed. When [14C]HCO3 w ...
Antioxidant Enzymes and Function
Antioxidant Enzymes and Function

... - monofunctional - peroxidatic activity only - not inducible by H2O 2 or Ascorbate - Increases during stationary phase of growth ...
6 - Beta-Sheet.org
6 - Beta-Sheet.org

... its sites appeared nearly identical with those occupied by the osmium derivative. Later cycles of phase refinement included all data to2 A resolution, since 2.0- to 2.5-A shell difference Patterson maps of the gold chloride and uranyl nitrate derivatives showed peaks 2 to 16 times above background a ...
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... Carbon and Its Functional Groups ...
Enzyme Catalysis - faculty at Chemeketa
Enzyme Catalysis - faculty at Chemeketa

... affinity for the substrate. 1. It does not compete with the substrate for the active site. 2. It does not need to resemble the structure of the substrate. 3. Its’ effect cannot be reversed by increasing the substrate concentration. ...
biologically important isotope hybrid
biologically important isotope hybrid

... are intimately connected, probably by the agency of a phenylalanine hydroxylase. Figure 9 illustrates the pmr spectrum of 2H-cytochrome c ('H-leucine) in the oxidized form. In comparison to the spectra of Figure 1, a very simple pattern indeed is obtained. Three methyl groups (tentative assignment) ...
Co-translational Targeting and Translocation of the Amino Terminus
Co-translational Targeting and Translocation of the Amino Terminus

... could target to the ER membrane and even translocate the amino terminus across without ongoing translation (29). In this work we examined the specific requirements for this process by removing components from the translation mix before the addition of ER membranes. As before, we generated RBOps by i ...
DIALYSIS and ELECTRODIALYSIS
DIALYSIS and ELECTRODIALYSIS

... Example: HF and HNO3 are often used as etching agents for stainless steel. In order to recover the acid, diffusion dialysis can be applied since the protons can pass the membrane but the Fe3+ ions can not. ...
Supplement I
Supplement I

... between cytosol and plastid and that pools are in near-equilibrium. Data are taken from the [U-13C6]-glucose labeling experiment. (a) GCMS fragments from compartmentspecific metabolites have very similar profiles even though they reflect different carbon compositions, indicating that all carbons are ...
Mechanisms of catalysis
Mechanisms of catalysis

... • Nucleophilic catalysis: donation of electrons from enzyme nucleophile to a substrate – side chains of His, Cys, Asp, Lys and Ser can participate in covalent catalysis by acting as nucleophiles ...
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Oxidative phosphorylation



Oxidative phosphorylation (or OXPHOS in short) is the metabolic pathway in which the mitochondria in cells use their structure, enzymes, and energy released by the oxidation of nutrients to reform ATP. Although the many forms of life on earth use a range of different nutrients, ATP is the molecule that supplies energy to metabolism. Almost all aerobic organisms carry out oxidative phosphorylation. This pathway is probably so pervasive because it is a highly efficient way of releasing energy, compared to alternative fermentation processes such as anaerobic glycolysis.During oxidative phosphorylation, electrons are transferred from electron donors to electron acceptors such as oxygen, in redox reactions. These redox reactions release energy, which is used to form ATP. In eukaryotes, these redox reactions are carried out by a series of protein complexes within the inner membrane of the cell's mitochondria, whereas, in prokaryotes, these proteins are located in the cells' intermembrane space. These linked sets of proteins are called electron transport chains. In eukaryotes, five main protein complexes are involved, whereas in prokaryotes many different enzymes are present, using a variety of electron donors and acceptors.The energy released by electrons flowing through this electron transport chain is used to transport protons across the inner mitochondrial membrane, in a process called electron transport. This generates potential energy in the form of a pH gradient and an electrical potential across this membrane. This store of energy is tapped by allowing protons to flow back across the membrane and down this gradient, through a large enzyme called ATP synthase; this process is known as chemiosmosis. This enzyme uses this energy to generate ATP from adenosine diphosphate (ADP), in a phosphorylation reaction. This reaction is driven by the proton flow, which forces the rotation of a part of the enzyme; the ATP synthase is a rotary mechanical motor.Although oxidative phosphorylation is a vital part of metabolism, it produces reactive oxygen species such as superoxide and hydrogen peroxide, which lead to propagation of free radicals, damaging cells and contributing to disease and, possibly, aging (senescence). The enzymes carrying out this metabolic pathway are also the target of many drugs and poisons that inhibit their activities.
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