The Reactive Sulfhydryl Groups of Microsomal Cytochrome Reductase
نویسندگان
چکیده
منابع مشابه
The reactive sulfhydryl groups of microsomal cytochrome reductase.
The results of previous work have indicated (2, 3) that one sulfhydryl group of microsomal cytochrome reductase is essential for the interaction of nucleotides with this enzyme. These results, however, do not rule out the possibility that there are other reactive sulfhydryl groups on the native enzyme and that they are involved directly or indirectly in nucleotide-enzyme interactions. In the ex...
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Under anaerobic conditions the addition of reduced diphosphopyridine nucleotide to stoichiometric amounts of microsomal cytochrome reductase yields reduced flavin and a nucleotideenzyme complex characterized by a 315-rnp absorption peak (2). The properties of the reactive sulfhydryl groups of the enzyme and the evidence for the participation of only one such group in this reaction have been des...
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In earlier work (1) a DPNH’-specific microsomal cytochrome reductase, liberated by alcohol extraction and partially purified, was identified in liver microsome fractions from rats and rabbits. Microsomal cytochrome, but not cytochrome c, was found to act as electron acceptor in the oxidation of DPNH catalyzed by the enzyme. Through a rapid cytochrome to cytochrome reaction, cytochrome c was red...
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S-Adenosylmethionine synthetase from Escherichia coli is rapidly inactivated by N-ethylmaleimide. In the presence of excess N-ethylmaleimide inactivation follows pseudo first-order kinetics, and loss of enzyme activity correlates with the incorporation of 2 eq of N-[ethyl-2-3H]maleimide/subunit. Preincubation of the enzyme with methionine and the ATP analog adenylylimidodiphosphate reduced the ...
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The biological role of reduced triphosphopyridine nucleotide (TPNH) and the metabolic pathways of its hydrogen atom and electron appear to be fundamentally different from those of reduced diphosphopyridine nucleotide (DPNH). The latter coenzyme appears to be intimately involved in cellular adenosine triphosphate (ATP) production, and is oxidized by both a phosphorylating, antimycin-sensitive pa...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1959
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)69755-8