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1: Science. 2007 Nov 30;318(5855):1461-4.
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Carbon dioxide activation at the Ni,Fe-cluster of anaerobic carbon monoxide dehydrogenase.

Jeoung JH, Dobbek H.

Laboratorium Proteinkristallographie and Forschungszentrum für Bio-Makromoleküle, Universität Bayreuth, D-95440 Bayreuth, Germany.

Anaerobic CO dehydrogenases catalyze the reversible oxidation of CO to CO2 at a complex Ni-, Fe-, and S-containing metal center called cluster C. We report crystal structures of CO dehydrogenase II from Carboxydothermus hydrogenoformans in three different states. In a reduced state, exogenous CO2 supplied in solution is bound and reductively activated by cluster C. In the intermediate structure, CO2 acts as a bridging ligand between Ni and the asymmetrically coordinated Fe, where it completes the square-planar coordination of the Ni ion. It replaces a water/hydroxo ligand bound to the Fe ion in the other two states. The structures define the mechanism of CO oxidation and CO2 reduction at the Ni-Fe site of cluster C.

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PMID: 18048691 [PubMed - indexed for MEDLINE]