Mass spectrometric determination of dioxygen bond splitting in the "peroxy" intermediate of cytochrome c oxidase

Marian Fabian; William W. Wong; Robert B. Gennis; Graham Palmer

doi:10.1073/pnas.96.23.13114

Mass spectrometric determination of dioxygen bond splitting in the "peroxy" intermediate of cytochrome c oxidase

Marian Fabian, William W. Wong, Robert B. Gennis, Graham Palmer

Biochemistry

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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 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.

Original language	English (US)
Pages (from-to)	13114-13117
Number of pages	4
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	96
Issue number	23
DOIs	https://doi.org/10.1073/pnas.96.23.13114
State	Published - Nov 9 1999

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Mass spectrometric determination of dioxygen bond splitting in the "peroxy" intermediate of cytochrome c oxidase. / Fabian, Marian; Wong, William W.; Gennis, Robert B. et al.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 96, No. 23, 09.11.1999, p. 13114-13117.

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N2 - 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.

AB - 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.

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Mass spectrometric determination of dioxygen bond splitting in the "peroxy" intermediate of cytochrome c oxidase

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