Cytochrome c oxidase is not a proton pump.
We conclude that the reduction of O2 to 2 H2O by cytochrome c oxidase of rat liver mitochondria involves the translocation of 4-from cytochrome c at the outer surface of the cristae membrane per O2 reduced and protonated by 4 H+ ions that enter the reaction domain from the inner aqueous phase. This net electron-translocating function of cytochrome c oxidase plugged through the mitochondrial cristae membrane is not linked to a proton-pumping function, such as that proposed by Wikström [7,8].
D000818:Animals; D000968:Antimycin A / Q000494:pharmacology; D001693:Biological Transport, Active; D003576:Electron Transport Complex IV / Q000378:metabolism*; D005295:Ferrocyanides; D008930:Mitochondria, Liver / Q000378:metabolism*; D010084:Oxidation-Reduction; D010101:Oxygen Consumption / Q000187:drug effects; D011522:Protons; D051381:Rats; D012402:Rotenone / Q000494:pharmacology
D005295:Ferrocyanides; D011522:Protons; D012402:Rotenone; D000968:Antimycin A; D003576:Electron Transport Complex IV