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• W2012159332 startingPage "491" @default.
• W2012159332 abstract "A significant lag in the thenoyltrifluoroacetone (TTFA)-sensitive succinate: ubiquinone reductase activity was observed when a ubiquinone-deficient resolved preparation of the enzyme was assayed in the presence of exogenous ubiquinone-2 (Q2) and 2,6-dichlorophenolindophenol. No such lag was seen when the free radical of N,N,N′,N′-tetramethyl-p-phenylenediamine (Wurster's Blue) was used as the terminal electron acceptor, or when the reduction of Q2 was directly measured. The apparent Km value for exogenous Q2 was determined in the Q2-mediated TTFA-sensitive succinate: Wurster's Blue reductase reaction. When the enzyme activity was measured directly by monitoring Q2 reduction without terminal acceptors, the time course of the reaction deviated from zero-order kinetics at Q2 concentrations which were much higher than those expected from the KQ2m value determined in the presence of Wurster's Blue. The time course of Q2 reduction fits a curve describing a competitive interrelationship between oxidized and reduced Q2 at the specific binding site. The data obtained are in agreement with the Q-pool behavior of ubiquinone in mitochondrial membranes and suggest that the rate of ubiquinone reduction by succinate is dependent on the QQH2 ratio." @default.
• W2012159332 created "2016-06-24" @default.
• W2012159332 creator A5074136986 @default.
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• W2012159332 date "1982-12-01" @default.
• W2012159332 modified "2023-09-25" @default.
• W2012159332 title "Kinetics of ubiquinone reduction by the resolved succinate: Ubiquinone reductase" @default.
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• W2012159332 doi "https://doi.org/10.1016/0005-2728(82)90065-2" @default.
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