通过质谱法测定细胞色素c氧化酶“过氧”中间体中的双氧键断裂情况。
Mass spectrometric determination of dioxygen bond splitting in the "peroxy" intermediate of cytochrome c oxidase.
作者信息
Fabian M, Wong W W, Gennis R B, Palmer G
机构信息
Department of Biochemistry, Rice University, Houston, TX 77005-1892, USA.
出版信息
Proc Natl Acad Sci U S A. 1999 Nov 9;96(23):13114-7. doi: 10.1073/pnas.96.23.13114.
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.
摘要
牛细胞色素c氧化酶的“过氧”中间体（P型）是通过在光解去除CO后，使双电子还原的混合价态CO复合物与(18)O(2)反应制备的。回收反应混合物中的水，并通过质谱分析其(18)O富集情况。结果发现，每当量的P型中大约有一个氧原子（(18)O）存在于大量水中。数据表明，在P中间体中氧-氧双氧键已经断裂，并且一个氧原子可以很容易地释放出来或与溶剂水中的氧进行交换。
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