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- W2128223485 abstract "An overview of the present knowledge about succinate:quinone oxidoreductase in Paracoccus denitrificans and Bacillus subtilis is presented. P. denitrificans contains a monoheme succinate:ubiquinone oxidoreductase that is similar to that of mammalian mitochondria with respect to composition and sensitivity to carboxin. Results obtained with carboxin-resistant P. denitrificans mutants provide information about quinone-binding sites on the enzyme and the molecular basis for the resistance. B. subtilis contains a diheme succinate:menaquinone oxidoreductase whose activity is dependent on the electrochemical gradient across the cytoplasmic membrane. Data from studies of mutant variants of the B. subtilis enzyme combined with available crystal structures of a similar enzyme, Wolinella succinogenes fumarate reductase, substantiate a proposed explanation for the mechanism of coupling between quinone reductase activity and transmembrane potential." @default.
- W2128223485 created "2016-06-24" @default.
- W2128223485 creator A5009593011 @default.
- W2128223485 date "2002-01-01" @default.
- W2128223485 modified "2023-10-16" @default.
- W2128223485 title "Succinate:quinone oxidoreductase in the bacteria Paracoccus denitrificans and Bacillus subtilis" @default.
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- W2128223485 doi "https://doi.org/10.1016/s0005-2728(01)00231-6" @default.
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