Carbon Dioxide Activation at the Ni,Fe-Cluster of Anaerobic Carbon Monoxide Dehydrogenase

  title={Carbon Dioxide Activation at the Ni,Fe-Cluster of Anaerobic Carbon Monoxide Dehydrogenase},
  author={Jae‐Hun Jeoung and Holger Dobbek},
  pages={1461 - 1464}
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… 
Structural basis of cyanide inhibition of Ni, Fe-containing carbon monoxide dehydrogenase.
The crystal structure of CODH-II from Carboxydothermus hydrogenoformans in complex with cyanide is reported and it is suggested that the competitive inhibitory character of cyanide originates from it obstruction of carbon monoxide binding to the nickel ion while the slow binding inhibition is due to a conformational change of the protein during which the water/hydroxo-ligand bound to iron is lost.
Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase
Using X-ray crystallography, unprecedented conformational dynamics in the C-cluster of the CODH from Desulfovibrio vulgaris are observed, providing the first view of an oxidized state of the cluster.
Mechanism of carbon monoxide oxidation at the active site [Ni-4Fe-5S] cluster of carbon monoxide dehydrogenase from Carboxydothermus hydrogenoformans
  • S. Ha
  • Chemistry, Biology
  • 2009
This research work focuses on the interaction of cluster C with CO analogue potassium cyanide and analysis of the resulting type of nickel coordination and on the effect of sodium sulfide on the enzymatic activities of the native CODHIICh.
Activation and reduction of carbon dioxide by nitrogenase iron proteins.
The Fe protein is established as a model for investigation of CO2 activation while suggesting its biotechnological adaptability for recycling the greenhouse gas into useful products.
In situ FTIR study of CO2 reduction on inorganic analogues of carbon monoxide dehydrogenase.
Intermediate species assignable to surface-bound CO2 and formyl groups were found to be stabilized in the presence of Ni, lending insight into its role in enhancing the multistep CO2 reduction process.
The extended reductive acetyl-CoA pathway: ATPases in metal cluster maturation and reductive activation
An overview of current knowledge on how ATPases achieve their tasks of maturation and reductive activation of acetyl-CoA is given.
Mechanism of Ni,Fe-Containing Carbon Monoxide Dehydrogenases
Phylogenetically diverse bacteria and archaea living under anaerobic conditions employ different classes of Ni,Fe-containing carbon monoxide dehydrogenases to use CO as an energy source or to contribute in converting CO2 to acetyl-CoA.
Energetics for the Mechanism of Nickel-Containing Carbon Monoxide Dehydrogenase.
It is suggested that the cluster has been over-reduced by X-rays and is therefore not the desired reduced state, which instead contains a bound CO on nickel, and it is concluded that one sulfide bridge in the Ni-Fe cluster should be protonated.
Metal-metal bonds in biology.
  • P. Lindahl
  • Chemistry
    Journal of inorganic biochemistry
  • 2012


Crystal Structure of a Carbon Monoxide Dehydrogenase Reveals a [Ni-4Fe-5S] Cluster
This structure represents the prototype for Ni-containing CO dehydrogenases from anaerobic bacteria and archaea and contains five metal clusters of which clusters B, B′, and a subunit-bridging, surface-exposed cluster D are cubane-type [4Fe-4S] clusters.
A Ni-Fe-Cu Center in a Bifunctional Carbon Monoxide Dehydrogenase/ Acetyl-CoA Synthase
A metallocofactor containing iron, sulfur, copper, and nickel has been discovered in the enzyme carbon monoxide dehydrogenase/acetyl-CoA (coenzyme A) synthase from Moorella thermoacetica and suggests a newly discovered role for copper in biology.
Carbon monoxide induced decomposition of the active site [Ni-4Fe-5S] cluster of CO dehydrogenase.
The CO oxidation activity of CODHII(Ch) is determined under different conditions of crystallization, prepared crystals of the enzyme in the presence of dithiothreitol or dithionite as reducing agents under an atmosphere of N(2) or CO, and solved the corresponding structures.
Interaction of Potassium Cyanide with the [Ni-4Fe-5S] Active Site Cluster of CO Dehydrogenase from Carboxydothermus hydrogenoformans*
A model of the CO oxidation mechanism at the [Ni-4Fe-5S] active site cluster of CODHIICh from C. hydrogenoformans is summarized and the square-planar coordination of nickel by 4S ligands is recovered, which includes the reformation of the Ni-(μ2S)-Fe1 bridge.
Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase
This x-ray structure of the anaerobic Ni-Fe-S carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum provides insight into the mechanism of biological CO oxidation and has broader significance for the roles of Ni and Fe in biological systems.
Carbon monoxide dehydrogenase from Rhodospirillum rubrum: effect of redox potential on catalysis.
Redox titration and stopped-flow kinetic experiments were performed to assess the previous results and conclusions, and activation did not correlate with reduction of Fe-S clusters in the enzyme, suggesting that the potential required for activation was milder than that required to reduce these clusters.
Effect of sodium sulfide on Ni-containing carbon monoxide dehydrogenases.
Effects of sulfide are analogous to those of other anions, including the substrate hydroxyl group, suggesting that these ions also bridge the Ni and unique Fe.
Reactivity of carbon monoxide dehydrogenase from Rhodospirillum rubrum with carbon dioxide, carbonyl sulfide, and carbon disulfide.
CO was a potent inhibitor of CO2 reduction at dissolved concentrations as low as 1 microM, but this inhibition could be prevented by quantitatively trapping CO as it was formed by including reduced hemoglobin in the assays.
Life with Carbon Monoxide
  • S. Ragsdale
  • Biology
    Critical reviews in biochemistry and molecular biology
  • 2004
The recently solved crystal structures of CODH and ACS along with spectroscopic measurements and computational studies provide insights into novel bio-organometallic catalytic mechanisms and into the nature of a 140 Å gas channel that coordinates the generation and utilization of CO.