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- W2069283762 abstract "The redox properties of flavin in active and non-active (oxaloacetate reacted) soluble succinate dehydrogenase were studied. Quantitative analysis of reductive activation titrations of redox titrations of active and non-active enzyme reveal that the redox potential of the histidylflavin in the active enzyme (−3 ± 15 mV) is high enough to allow reduction by succinate, whereas in the non active enzyme it is −196 ± 19 mV, far to low to be reduced by substrate. The flavin radical in the active enzyme attains 60% of total flavin at a poised redox potential of about +60 mV, upon addition of oxaloacetate the magnitude of the signal is diminished and the potential where it reaches maximal concentration is shifted by about −200 mV. A mechanism is proposed which ascribes the fundamental difference between active and non-active enzyme to the inability of the latter to be reduced by substrate." @default.
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- W2069283762 date "1980-07-01" @default.
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- W2069283762 title "Modulation of the flavin redox potential as mode of regulation of succinate dehydrogenase activity" @default.
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- W2069283762 doi "https://doi.org/10.1016/0005-2728(80)90171-1" @default.
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