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

被引：105

作者：

Fabian, M

Wong, WW

Gennis, RB

Palmer, G ^{[1
]}

机构：

[1] Rice Univ, Dept Biochem & Cell Biol, Houston, TX 77251 USA

[2] Baylor Univ, USDA ARS, Childrens Nutr Res Ctr, Coll Med,Dept Pediat, Houston, TX 77030 USA

[3] Univ Illinois, Dept Biochem, Urbana, IL 61801 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1999年 / 96卷 / 23期

关键词：

D O I：

10.1073/pnas.96.23.13114

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The "peroxy" intermediate (P form) of bovine cytochrome c oxidase was prepared by reaction of the two-electron reduced mixed-valence CO complex with O-18(2) after photolytic removal of CO. The water present in the reaction mixture was recovered and analyzed for O-18 enrichment by mass spectrometry, It was found that approximately one oxygen atom (O-18) 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.

引用

页码：13114 / 13117

页数：4

共 38 条

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