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• W2091648596 abstract "1. The intracellular location and function of TPNH: cytochrome c reductase (EC 1.6.2.3) and of DPNH; cytochrome c reductase system in the yeast cell have been investigated. 2. Both enzyme activities are associated with particles. 3. Homogenates of anaerobically grown yeast and of the “petite” mutant, both of which are unable to respire, exhibit practically the same specific TPNH: cytochrome c reductase activity as homogenates of respiring baker's yeast. TPNH: cytochrome c reductase activity in antimycin-insensitive, does not interact with endogenous cytochrome c of yeast mitochondria and is predominantly associated with microsomal particles which have not yet been described for yeast. Electron micrographs of these particles are presented. 4. In contrast, DPNH: cytochrome c reductase activity, which is greatly lowered in homogenates of anaerobic or “peptide” mutant yeast, is 95% inhibited by antimycin and interacts rapidly with endogenous cytochrome c of yeast mitochondria. More than 95% of this reductase activity is mitochondrial, the remainder being located in microsomes. Microsomal DPNH: cytochrome c reductase activity is not inhibited by antimycin. 5. It is concluded, that TPNH: cytochrome c reductase of Saccharomyces cerevisine is not a respiratory-chain enzyme. Some implications of these findings are discussed." @default.
• W2091648596 created "2016-06-24" @default.
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• W2091648596 date "1964-03-01" @default.
• W2091648596 modified "2023-10-16" @default.
• W2091648596 title "Triphosphopyridine nucleotide: cytochrome C reductase of Saccharomyces Cerevisiae a “microsomal” enzyme" @default.
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• W2091648596 doi "https://doi.org/10.1016/0926-6569(64)90130-0" @default.
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