3B52

Ni,Fe-CODH-600 mV state + CO2

Summary for 3B52

• Entry DOI: 10.2210/pdb3b52/pdb
• Related: 3B51 3B53
• Descriptor: Carbon monoxide dehydrogenase 2, FE (II) ION, IRON/SULFUR CLUSTER, ... (7 entities in total)
• Functional Keywords: cluster c, 4fe-4s, cytoplasm, iron, iron-sulfur, membrane, metal-binding, nickel, oxidoreductase
• Biological source: Carboxydothermus hydrogenoformans Z-2901
• Cellular location: Cytoplasm: Q9F8A8
• Total number of polymer chains: 1
• Total formula weight: 70173.69

Authors

Jeoung, J.H.,Dobbek, H. (deposition date: 2007-10-25, release date: 2007-12-11, Last modification date: 2024-02-21)

Primary citation

Jeoung, J.H.,Dobbek, H.
Carbon dioxide activation at the Ni,Fe-cluster of anaerobic carbon monoxide dehydrogenase.
Science, 318:1461-1464, 2007

PubMed Abstract: 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.

PubMed: 18048691
DOI: 10.1126/science.1148481

Experimental method

X-RAY DIFFRACTION (1.5 Å)