[Activation of complex I in the reaction of NADH oxidation and delta mu H+-dependent NAD+ reduction by succinate].
Complex I catalyzed the NADH-oxidase and NADH-Q reductase reactions with a pH-dependent lag-phase. The enzyme activated during a short-term aerobic incubation remained active for a relatively long period of time (tens of minutes at 25 degrees C). Similar NADH-induced slow changes in the activity of the reverse electron transfer were found earlier in our laboratory. The synchronous change of the enzyme activity in the forward and reverse directions points to the existence of the slowly interconverting states of complex I, namely, an active state catalyzing the NADH oxidation and delta mu H(+)-dependent NAD+ reduction and an inactive state.
Kotliar
A B
AB
D000818:Animals; D002417:Cattle; D004579:Electron Transport; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008929:Mitochondria, Heart / Q000201:enzymology / Q000378:metabolism; D009243:NAD / Q000378:metabolism*; D016660:NAD(P)H Dehydrogenase (Quinone); D010084:Oxidation-Reduction; D011808:Quinone Reductases / Q000378:metabolism*; D013367:Submitochondrial Particles / Q000201:enzymology* / Q000378:metabolism; D013386:Succinates / Q000378:metabolism*
D013386:Succinates; D009243:NAD; D016660:NAD(P)H Dehydrogenase (Quinone); D011808:Quinone Reductases
Aktivatsiia kompleksa I v reaktsii okisleniia NADH i v delta mu H+- zavisimom vosstanovlenii NAD+ suktsinatom.