Dehydrogenase kinetic parameters determine the electron competition mechanisms in respiratory chain
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چکیده
منابع مشابه
The NADH Dehydrogenase of the Respiratory Chain of Escherichia coli
The NADH dehydrogenase of the Escherichiu coli respiratory chain has been identified by the following properties: (a) its location in membrane vesicles; (b) its inhibition by AMP in a fashion similar to that of the NADH oxidase; (c) its specificity for NADH, but not NADPH, with the same K, for NADH as that of the NADH oxidase; (d) its sensitivity when membrane-bound to inhibition by dicoumarol,...
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Rhein (4,5-dibydroxyanthraquinone-Z-carboxylic acid) inhibits the mitochondrial oxidation of reduced nicotamide adenine dinucleotide (NADH) but not of succinate. The inhibition is competitive with respect to substrate and involves a block between NADH and the flavin of NADH dehydrogenase. The Ki is about 2 ~.LM at 30”. Evidence for this localization has come from kinetic analysis of the effect ...
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We show that the rate at which electrons pass through the respiratory chain in mitochondria and respiring prokaryotic cells is described by the product of three terms, one describing electron donation, one acceptance, and a third, the thermodynamic drive. We apply the theory of nonequilibrium thermodynamics in the context of the chemiosmotic model of proton translocation and energy conservation...
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The pyruvate dehydrogenase (PDH) multienzyme complex plays a key role in the metabolic interconnection between glycolysis and the citric acid cycle. Transcription of the Escherichia coli genes for all three components of the PDH complex in the pdhR-aceEF-lpdA operon is repressed by the pyruvate-sensing PdhR, a GntR family transcription regulator, and derepressed by pyruvate. After a systematic ...
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Pteridine reductase 1 (PTR1) is a novel broad spectrum enzyme of pterin and folate metabolism in the protozoan parasite Leishmania. Overexpression of PTR1 confers methotrexate resistance to these protozoa, arising from the enzyme's ability to reduce dihydrofolate and its relative insensitivity to methotrexate. The kinetic mechanism and stereochemical course for the catalyzed reaction confirm PT...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Bioenergetics
سال: 2012
ISSN: 0005-2728
DOI: 10.1016/j.bbabio.2012.06.346