Organometallic iron: the key to biological hydrogen metabolism

被引：100

作者：

Adams, MWW ^{[1
]}

Stiefel, EI

机构：

[1] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA

[2] ExxonMobil Res & Engn Co, Corp Strateg Res, Annandale, NJ 08801 USA

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 2000年 / 4卷 / 02期

关键词：

D O I：

10.1016/S1367-5931(99)00077-0

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：

X-ray crystallography of iron-hydrogenases reveals that the active-site H-cluster contains an unmistakably organometallic dinuclear iron subcluster. The nickel-hydrogenases, which in general play different metabolic roles, have a distinct but related active-site structure. The new structural definition, combined with chemical analogs and theoretical treatment, points toward mechanistic understanding of iron-hydrogenases and the possibility of a unified mechanism for all hydrogenases.

引用

页码：214 / 220

页数：7

共 71 条

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