Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster

被引：437

作者：

Dobbek, H

Svetlitchnyi, V

Gremer, L

Huber, R

Meyer, O

机构：

[1] Max Planck Inst Biochem, Abt Strukturforsch, D-82152 Martinsried, Germany

[2] Univ Bayreuth, Bayreuther Zentrum Mol Biowissensch, D-95440 Bayreuth, Germany

[3] Univ Bayreuth, Lehrstuhl Mikrobiol, D-95440 Bayreuth, Germany

来源：

SCIENCE | 2001年 / 293卷 / 5533期

关键词：

D O I：

10.1126/science.1061500

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The homodimeric nickel-containing CO dehydrogenase from the anaerobic bacterium Carboxydothermus hydrogenoformans catalyzes the oxidation of CO to CO2. A crystal structure of the reduced enzyme has been solved at 1.6 angstrom resolution. This structure represents the prototype for Ni-containing CO dehydrogenases from anaerobic bacteria and archaea. It contains five metal clusters of which clusters B, B', and a subunit-bridging, surface-exposed cluster D are cubane-type [4Fe-4S] clusters. The active-site clusters C and C' are novel, asymmetric [Ni-4Fe-5S] clusters. Their integral Ni ion, which is the likely site of CO oxidation, is coordinated by four sulfur ligands with square planar geometry.

引用

页码：1281 / 1285

页数：5

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