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The catalytic properties of pulsed and resting cytochrome c oxidase (ferrocytochrome c: oxygen oxidoreductase, EC 1.9.3.1), expressed in terms of a minimal kinetic scheme and simulated by numerical computations, were successfully described. A two-state model, in which the relative amounts of the enzyme present in each conformation are regulated by the rates of electron flux and O2 binding on one side and the interconversion rates on the other, accounts for the activation of cytochrome c oxidase during turnover.
Wilson et al. (Sun,) studied this question.