A functional model of the cytochrome c oxidase active site:: Unique conversion of a heme-μ-peroxo-CuII intermediate into heme-superoxo/CuI

被引：65

作者：

Liu, JG ^{[1
]}

Naruta, Y ^{[1
]}

Tani, F ^{[1
]}

机构：

[1] Kyushu Univ, Inst Mat Chem & Engn, Higashi Ku, Fukuoka 8128581, Japan

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2005年 / 44卷 / 12期

关键词：

copper; heme proteins; iron; metalloenzymes; oxidoreductases;

D O I：

10.1002/anie.200462582

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

(Chemical Equation Presented) Axial ligation of the heme moiety by a proximal imidazole group is observed in a novel cytochromec oxidase (CcO) active-site model 1 in which the copper ion is bound to a N-(2-hydroxyphenyl) imidazole moiety. Spectroscopic observations of 1 suggest the unique transformation of an initial heme-μ-peroxo-CuII species into a heme-superoxide/CuI intermediate in the course of the CcO oxygenation reaction at low temperature. © 2005 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：1836 / 1840

页数：5

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