Cytochrome c oxidase: decay of the primary oxygen intermediate involves direct electron transfer from cytochrome a.
The decay of the primary intermediate generated in the reaction of oxygen with cytochrome c oxidase is nearly one order of magnitude faster in the fully reduced form of the enzyme than it is in the mixed valence form. To account for this observation, we propose a model describing the early molecular events in the reaction. In this model the decay of the primary Fe-O2 intermediate in the fully reduced enzyme is a consequence of direct electron transfer from cytochrome a. To test the model we measured the time dependence of the oxidation of cytochrome a by monitoring the resonance Raman scattering intensity of its vibrational modes. A rapid oxidation of cytochrome a was detected that quantitatively agrees with the model. These results indicate that the mechanism of oxygen reduction and proposed frameworks for proton translocation must be reexamined.
Han
S H
SH
AT&T Bell Laboratories, Murray Hill, NJ 07974.
Ching
Y C
YC
Rousseau
D L
DL
D000818:Animals; D002417:Cattle; D003198:Computer Simulation; D017936:Cytochrome a Group; D003574:Cytochrome c Group / Q000378:metabolism; D003580:Cytochromes / Q000378:metabolism*; D004579:Electron Transport; D003576:Electron Transport Complex IV / Q000378:metabolism*; D007700:Kinetics; D008962:Models, Theoretical; D009206:Myocardium / Q000201:enzymology; D010084:Oxidation-Reduction; D010101:Oxygen Consumption; D013059:Spectrum Analysis, Raman; D013997:Time Factors
D017936:Cytochrome a Group; D003574:Cytochrome c Group; D003580:Cytochromes; D003576:Electron Transport Complex IV