Mass spectrometric determination of dioxygen bond splitting in the “peroxy” intermediate of cytochrome c oxidase
AUTOR(ES)
Fabian, Marian
FONTE
The National Academy of Sciences
RESUMO
The “peroxy” intermediate (P form) of bovine cytochrome c oxidase was prepared by reaction of the two-electron reduced mixed-valence CO complex with 18O2 after photolytic removal of CO. The water present in the reaction mixture was recovered and analyzed for 18O enrichment by mass spectrometry. It was found that approximately one oxygen atom (18O) 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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=23909Documentos Relacionados
- Dioxygen activation and bond cleavage by mixed-valence cytochrome c oxidase
- Elevated Proton Leak of the Intermediate OH in Cytochrome c Oxidase
- The structure of the paramagnetic oxygen intermediate in the cytochrome c oxidase reaction.
- Primary intermediate in the reaction of oxygen with fully reduced cytochrome c oxidase.
- Cytochrome c oxidase: decay of the primary oxygen intermediate involves direct electron transfer from cytochrome a.
