title: Mass spectrometric determination of dioxygen bond splitting in the "peroxy" intermediate of cytochrome c oxidase.
abstract: The "peroxy" intermediate (P form) of bovine cytochrome c oxidase was prepared by reaction of the two-electron reduced mixed-valence CO complex with (18)O(2) after photolytic removal of CO. The water present in the reaction mixture was recovered and analyzed for (18)O enrichment by mass spectrometry. It was found that approximately one oxygen atom ((18)O) per one equivalent of the P form was present in the bulk water. The data show that the oxygen-oxygen dioxygen bond is already broken in the P intermediate and that one oxygen atom can be readily released or exchanged with the oxygen of the solvent water.
authors.affiliation: Department of Biochemistry, Rice University, Houston, TX 77005-1892, USA.
authors.forename: M
authors.initials: M
authors.lastname: Fabian
authors.forename: W W
authors.initials: WW
authors.lastname: Wong
authors.forename: R B
authors.initials: RB
authors.lastname: Gennis
authors.forename: G
authors.initials: G
authors.lastname: Palmer
mesh_terms: D000818:Animals; D002417:Cattle; D003576:Electron Transport Complex IV / Q000737:chemistry*; D013058:Mass Spectrometry; D010100:Oxygen / Q000737:chemistry*; D010231:Paracoccus denitrificans / Q000201:enzymology
chemical_list: D003576:Electron Transport Complex IV; D010100:Oxygen