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- W1992346119 abstract "The mitochondrial NADH dehydrogenase catalyzes a one-electron reduction of quinones. Semiquinones thus formed have the hyperfine structures of their free anion radicals and are suggested to be detached from the enzyme. In the presence of suitable electron acceptors electron transfer occurs from the semiquinone to the acceptor. The mechanism of quinone reduction by spinach ferredoxin-NADP reductase is the same as that by the NADH dehydrogenase. On the other hand, the NAD(P)H dehydrogenase (DT-diaphorase) prepared from liver soluble fraction catalyzes a typical two-electron reduction of quinones such as p-benzoquinone and 2-methyl-1,4-naphthoquinone. The mechanisms of one-electron and two-electron reduction of quinones are readily distinguishable by the use of an electron spin resonance spectrometer equipped with a flow apparatus and also by the use of an appropriate set of electron acceptors. It is concluded that the reduction of quinones and oxygen by flavoproteins falls into three mechanistic categories: one-electron, two-electron and mixed-type reactions." @default.
- W1992346119 created "2016-06-24" @default.
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- W1992346119 date "1970-09-01" @default.
- W1992346119 modified "2023-10-12" @default.
- W1992346119 title "One-electron-transfer reactions in biochemical systems V. Difference in the mechanism of quinone reduction by the NADH dehydrogenase and the NAD(P)H dehydrogenase (DT-diaphorase)" @default.
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- W1992346119 doi "https://doi.org/10.1016/0005-2728(70)90220-3" @default.
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