Chemistry relating to the nickel enzymes CODH and ACS

被引：62

作者：

Evans, DJ ^{[1
]}

机构：

[1] John Innes Inst, Dept Biol Chem, Norwich NR4 7UH, Norfolk, England

来源：

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

基金：

英国生物技术与生命科学研究理事会;

关键词：

carbon monoxide dehydrogenase; acetyl-CoA synthase; nickel enzymes;

D O I：

10.1016/j.ccr.2004.09.012

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

The nickel enzymes CODH and ACS (carbon monoxide dehydrogenase and acetyl-CoA synthase), as found in for example Moorella thermoacetica (formerly Clostridium thermoaceticum), play an important role in carbon cycling: the enzymes convert carbon dioxide through to cell carbon. CODH and ACS are neither structurally nor functionally related to NiFe-hydrogenase, other than that all three enzymes contain assemblies of iron, nickel and sulfur at their active sites. However, the coordination chemistry of synthetic compounds that show structural or functional analogy to the enzyme active sites has been developed in parallel. Herein will be described mono-, di- and multi-nuclear metallic complexes of relevance to the metallocentres of CODH and ACS. (c) 2004 Elsevier B.V. All rights reserved.

引用

页码：1582 / 1595

页数：14

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