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Humboldt-Universitaet zu Berlin - Structural Biology / Biochemistry

Humboldt-Universitaet zu Berlin | Department of Biology | Structural Biology / Biochemistry | Publications | Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster

Holger Dobbek, Vitali Svetlitchnyi, Lothar Gremer, Robert Huber, and Ortwin Meyer (2001)

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

Science, 293(5533):1281–1285.

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.