The effect of rate limitation by cytochrome c on the redox state of the ubiquinone pool in reconstituted NADH: cytochrome c reductase.
The kinetic model of Ragan & Cottingham [(1985) Biochim. Biophys. Acta 811, 13-31] for electron transport through a mobile pool of quinone predicts that, under certain conditions, the normal linear dependence of electron flow on the degree of reduction (or oxidation) of the quinone should no longer be found. These conditions can be met by reconstituted NADH: cytochrome c reductase (Complex I-III from bovine heart) when electron flow is rate-limited by a low concentration of cytochrome c. We show that, in such a system, the dependence of activity (varied by inhibition with rotenone) on the steady-state level of quinone reduction is indeed non-linear and very closely accounted for by the theory.
Reed
J S
JS
Department of Biochemistry, University of Southampton, U.K.
Ragan
C I
CI
D000818:Animals; D002417:Cattle; D003579:Cytochrome Reductases / Q000378:metabolism*; D003574:Cytochrome c Group / Q000378:metabolism*; D004579:Electron Transport; D007700:Kinetics; D008689:Methacrylates; D008956:Models, Chemical; D009245:NADH Dehydrogenase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D010084:Oxidation-Reduction; D012402:Rotenone / Q000494:pharmacology; D013844:Thiazoles / Q000494:pharmacology; D014451:Ubiquinone / Q000378:metabolism*
D003574:Cytochrome c Group; D008689:Methacrylates; D013844:Thiazoles; D012402:Rotenone; D014451:Ubiquinone; C030517:myxothiazol; D003579:Cytochrome Reductases; D009245:NADH Dehydrogenase