The structure of the paramagnetic oxygen intermediate in the cytochrome c oxidase reaction.
A paramagnetic intermediate with an unusual e.p.r. spectrum is formed when fully reduced cytochrome c oxidase is allowed to react with dioxygen at 173 K. The effect on the e.p.r. spectrum of using dioxygen enriched in 17O was investigated. These experiments show that an oxygen atom derived from dioxygen is bound to Cu2+ in the intermediate. The e.p.r. parameters can be explained in terms of a weak antiferromagnetic interaction (J approximately equal to 10 cm-1) between Cu2+B and cytochrome a3 in the low-spin ferryl ion state. It is suggested that an OH- ion bound to Cu2+B is hydrogen bonded to the oxygen atom of the ferryl ion in cytochrome a3.
D000818:Animals; D002417:Cattle; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods; D003576:Electron Transport Complex IV / Q000378:metabolism*; D008929:Mitochondria, Heart / Q000201:enzymology*; D010084:Oxidation-Reduction; D010103:Oxygen Isotopes; D011485:Protein Binding
D010103:Oxygen Isotopes; D003576:Electron Transport Complex IV