Abstract
Kinetic studies of the electron transfer processes performed by cytochrome oxidase have assigned rates of electron transfer between the metal centers involved in the oxidation of ferrocytochromec by molecular oxygen. Transient-state studies of the reaction with oxygen have led to the proposal of a sequence of carriers from cytochromec, to CuA, to cytochromea, and then to the binuclear (i.e., cytochromea 3-CuB) center. Electron exchange rates between these centers agree with relative center-to-center distances as follows; cytochromec to CuA 5–7 Å, cytochromec to cytochromea 20–25 Å, CuA to cytochromea 14–16 Å and cytochromea to cytochrome a3-CuB 8–10 Å. It is proposed that the step from cytochromea to the binuclear center is the key control point in the reaction and that this step is one of the major points of energy transduction in the reaction cycle.

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