The effect of oxygen concentration on the steady-state kinetics of the solubilized cytochrome c oxidase.
1. The steady-state kinetics of ascorbate oxidation as a function of oxygen concentration was measured with a solubilized cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1) preparation. 2. Linear double reciprocal plots were obtained at various fixed concentrations of ascrobate, cytochrome c and cytochrome aa3. 3. The results are interpreted in terms of an oxidase model similar to that put forward by Minnaert in 1961 (Minnaert, K. (1961) Biochim. Biophys. Acta 50, 23-34). 4. The Km for oxygen at infinite cytochrome c concentration is 0.95 muM and the intramolecular rate constant for the transfer of electrons from cytochrome c to cytochome aa3 is 400 s(-1). According to the model, this implies that the second order rate constant for the reaction between oxygen and the oxidase is 9.5 X 10(7)M(-1)-s(-1).
D000818:Animals; D001205:Ascorbic Acid; D002417:Cattle; D003576:Electron Transport Complex IV / Q000378:metabolism*; D007700:Kinetics; D008433:Mathematics; D008931:Mitochondria, Muscle / Q000201:enzymology; D009206:Myocardium; D010101:Oxygen Consumption
D003576:Electron Transport Complex IV; D001205:Ascorbic Acid