H+/e stoichiometry of mitochondrial cytochrome complexes reconstituted in liposomes Rate‐dependent changes of the stoichiometry in the cytochrome c oxidase vesicles

Abstract
The H+/e stoichiometry of protonmotive cytochrome c oxidase, isolated from bovine heart mitochondria and reconstituted in liposomes, has been determined by making use of direct spectrophotometric measurements of the initial rates of e flow and H+ translocation. It is shown that the ←H+/e ratio for redox‐linked proton ejection by the oxidase varies from around 0 to a maximum of 1 as a function of the rate of overall electron flow in the complex.