Anomalies in the polarographic measurement of cytochrome oxidase activity.
Reaction kinetics of the reduction of O2 by cytochrome oxidase follow essentially the same rate equation as that proposed for the oxidation of cytochrome c. However, the apparent second order rate constant varies with the oxidase concentration. The redox level of cytochrome c at the steady state was found to be essentially temperature-independent. Currently recognized pathways (or mechanisms) of electron transport from cytochrome c to O2 do not predict, and cannot account for the occurrence of these phenomena.
D000818:Animals; D002417:Cattle; D003574:Cytochrome c Group / Q000378:metabolism; D003576:Electron Transport Complex IV / Q000378:metabolism*; D007700:Kinetics; D009206:Myocardium / Q000201:enzymology; D010084:Oxidation-Reduction; D011048:Polarography / Q000379:methods; D013696:Temperature
D003574:Cytochrome c Group; D003576:Electron Transport Complex IV