Evidence for a ferryl Fea3 in oxygenated cytochrome c oxidase.
Evidence is reported which shows that a reactive ferryl Fea3/cupric CuB binuclear couple is present at the dioxygen reduction site in "oxygenated" cytochrome c oxidase; when the fully reduced enzyme is reoxidized at low temperatures; and when partially reduced cytochrome c oxidase is reoxidized with dioxygen at room temperature.
D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D003300:Copper / Q000378:metabolism; D004578:Electron Spin Resonance Spectroscopy; D003576:Electron Transport Complex IV; D005290:Ferric Compounds; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism; D013053:Spectrophotometry; D013696:Temperature
D005290:Ferric Compounds; D003300:Copper; D003576:Electron Transport Complex IV; D010100:Oxygen