Respiratory chain-linked NADH dehydrogenase. Mechanisms of assembly.
نویسندگان
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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The membranes of the thermoacidophilic archaeon Sulfolobus metallicus exhibit an oxygen consumption activity of 0.5 nmol O(2) min(-1) mg(-1), which is insensitive to rotenone, suggesting the presence of a type-II NADH dehydrogenase. Following this observation, the enzyme was purified from solubilised membranes and characterised. The pure protein is a monomer with an apparent molecular mass of 4...
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Purified preparations of the reduced nicotinamide adenine dinucleotide dehydrogenase of the respiratory chain, extracted with the aid of phospholipase at moderate temperature, do not catalyze the reduction of long chain coenzyme Q derivatives (Q6 and QIO) at significant rates and are not inhibited by amytal or rotenone. On exposure of the enzyme to conditions which have been used for the extrac...
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The finding that ferredoxin and photosynthetic pyridine nucleotide reductase contain approximately equimolar amounts of “labile” sulfide and nonheme iron, and that both of these components are liberated in inorganic form with attendant inactivation upon acid treatment of these proteins (3-5), has stimulated considerable interest in the chemical nature and function of labile sulfide in oxidizing...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1990
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)46248-x