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 ferrocytochrome c by molecular oxygen. Transient-state studies of the reaction with oxygen have led to the proposal of a sequence of carriers from cytochrome c, to CuA, to cytochrome a, and then to the binuclear (i.e., cytochrome a3-CuB) center. Electron exchange rates between these centers agree with relative center-to-center distances as follows; cytochrome c to CuA 5-7 A, cytochrome c to cytochrome a 20-25 A, CuA to cytochrome a 14-16 A and cytochrome a to cytochrome a3-CuB 8-10 A. It is proposed that the step from cytochrome a 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.