Active sites of transition-metal enzymes with a focus on nickel

被引:110
作者
Ermler, U
Grabarse, W
Shima, S
Goubeaud, M
Thauer, RK
机构
[1] Max Planck Inst Biophys, D-60528 Frankfurt, Germany
[2] Univ Marburg, Max Planck Inst Terr Mikrobiol, D-35043 Marburg, Germany
[3] Univ Marburg, Mikrobiol Lab, D-35043 Marburg, Germany
关键词
D O I
10.1016/S0959-440X(98)80095-X
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
Since 1995, crystal structures have been determined for many transition-metal enzymes, in particular those containing the rarely used transition metals vanadium, molybdenum, tungsten, manganese, cobalt and nickel. Accordingly, our understanding of how an enzyme uses the unique properties of a specific transition metal has been substantially increased in the past few years. The different functions of nickel in catalysis are highlighted by describing the active sites of six nickel enzymes - methyl-coenyzme M reductase, urease, hydrogenase, superoxide dismutase, carbon monoxide dehydrogenase and acetyl-coenzyme A synthase.
引用
收藏
页码:749 / 758
页数:10
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