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.
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收藏
页码：214 / 220
页数：7
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