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Science 17 August 2001:
Vol. 293. no. 5533, pp. 1281 - 1285
DOI: 10.1126/science.1061500
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Research Articles

Crystal Structure of a Carbon Monoxide Dehydrogenase Reveals a [Ni-4Fe-5S] Cluster

Holger Dobbek,1* Vitali Svetlitchnyi,2* Lothar Gremer,2 Robert Huber,1 Ortwin Meyer23*

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.

1 Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D-82152 Martinsried, Germany.
2 Lehrstuhl für Mikrobiologie and
3 Bayreuther Zentrum für Molekulare Biowissenschaften (BZMB), Universität Bayreuth, D-95440 Bayreuth, Germany.
*   To whom correspondence should be addressed. E-mail: dobbek{at}biochem.mpg.de, vitali.svetlitchnyi{at}uni-bayreuth.de, ortwin.meyer{at}uni-bayreuth.de.

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