Structure-function relationships of nickel-iron sites in hydrogenase and a comparison with the active sites of other nickel-iron enzymes

被引：88

作者：

Volbeda, A ^{[1
]}

Fontecilla-Camps, JC ^{[1
]}

机构：

[1] UJF, CNRS, CEA, Inst Biol Struct JP Ebel,Lab Cristallog & Cristal, F-38027 Grenoble, France

来源：

COORDINATION CHEMISTRY REVIEWS | 2005年 / 249卷 / 15-16期

关键词：

hydrogenase; nickel-iron-sulfur clusters; gas metabolism; carbon monoxide dehydrogenase; acetyl coenzyme A synthase;

D O I：

10.1016/j.ccr.2004.12.009

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

Recent studies of [NiFe]-hydrogenases have provided a significant amount of new structural and kinetic data on the many states the active site displays upon enzyme inhibition, its activation and during catalysis. Other Ni-Fe containing active sites have been found in the bifunctional carbon monoxide dehydrogenase/acetyl coenzyme A synthase that is involved in anaerobic carbon fixation through the Wood-Ljungdahl pathway. Here, we discuss the influence of the protein environment on the reactivity of these three active sites and analyze the differences and similarities in their structural and chemical properties. (c) 2004 Elsevier B.V. All rights reserved.

引用

页码：1609 / 1619

页数：11

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