Comparative studies in series of cytochrome c oxidase models

被引:12
作者
Melin, F. [1 ]
Trivella, A.
Lo, M. [1 ]
Ruzie, C. [2 ]
Hijazi, I. [2 ]
Oueslati, N.
Wytko, J. A. [1 ]
Boitrel, B. [2 ]
Boudon, C. [3 ]
Hellwig, P.
Weiss, J. [1 ]
机构
[1] Univ Strasbourg, CNRS, UMR 7177, Inst Chim Strasbourg,CLAC, F-67000 Strasbourg, France
[2] Univ Rennes 1, CNRS, UMR 6226, F-35042 Rennes, France
[3] Univ Strasbourg, CNRS, UMR 7177, Inst Chim Strasbourg,Lab Electrochim Chim Phys Co, F-67000 Strasbourg, France
关键词
ELECTROCATALYTIC REDUCTION; INFRARED-SPECTROSCOPY; SYNTHETIC MODELS; ADDUCT FORMATION; HEME; DIOXYGEN; COORDINATION; PORPHYRINS; COMPLEXES; IRON(II);
D O I
10.1016/j.jinorgbio.2011.11.016
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
This study compares the behavior as cytochrome c oxidase (CcO) functional and structural models of a series of reported and unreported ligands that provide either a binding site for copper without a built-in proximal base, or both a flexible binding site for copper and a built-in proximal base, or a fixed binding site for copper with a built-in proximal base. The comparisons of the models show that the relative position of the two metal sites is not only a crucial parameter in the control of the catalytic behavior but also essential in mimicking other features of the enzyme such as CO exchange between the ferrous heme a(3) and the cuprous Cu-B center. (C) 2011 Elsevier Inc. All rights reserved.
引用
收藏
页码:196 / 202
页数:7
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