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

  title={Crystal Structure of a Carbon Monoxide Dehydrogenase Reveals a [Ni-4Fe-5S] Cluster},
  author={Holger Dobbek and Vitali A. Svetlitchnyi and Lothar Gremer and Robert Huber and Ortwin Meyer},
  pages={1281 - 1285}
The homodimeric nickel-containing CO dehydrogenase from the anaerobic bacterium Carboxydothermus hydrogenoformanscatalyzes 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… 
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 Dioxide Activation at the Ni,Fe-Cluster of Anaerobic Carbon Monoxide Dehydrogenase
The structures define the mechanism of CO oxidation and CO2 reduction at the Ni-Fe site of cluster C, where CO2 acts as a bridging ligand between Ni and the asymmetrically coordinated Fe, where it completes the square-planar coordination of the Ni ion.
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.
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.
The metalloclusters of carbon monoxide dehydrogenase/acetyl-CoA synthase: a story in pictures
Recent studies have revealed Ni-Ni to be the active state, unveiled the source of the heterogeneity that had plagued studies of CODH/ACS for decades, and produced a metal-replacement strategy to generate highly active and nearly homogeneous enzyme.
The methanogenic CO2 reducing-and-fixing enzyme is bifunctional and contains 46 [4Fe-4S] clusters
The structural details of a CO2 reducing enzyme reveal long-distance coupling of active sites and tungsten redox centers, and the arrangement of [4Fe-4S] clusters functions as an electron relay but potentially also couples the four tungstopterin active sites over 206 angstroms.
Maturation of the [Ni–4Fe–4S] active site of carbon monoxide dehydrogenases
It is questioned the conception that the maturation of all CODH depends on the accessory protein CooC described as essential for nickel insertion into the active site, and the available literature reveals biological variations in C ODH active site biosynthesis.
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.
Structural bases for the catalytic mechanism of Ni-containing carbon monoxide dehydrogenases.
This work proposes a catalytic cycle that is consistent with both observations and stereochemistry, and gives alternatives to one of the most difficult aspects of the cycle, namely, the location of the two electrons in the most reduced state of the C-cluster.


Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine.
A mechanism based on a structure with the bound suicide-substrate cyanide is suggested and displays the necessity of S-selanylcysteine for the catalyzed reaction.
The Role of Se, Mo and Fe in the Structure and Function of Carbon Monoxide Dehydrogenase
CO dehydrogenase is a selenium-containing molybdo-iron-sulfur-flavoenzyme, which has been crystallized and structurally characterized in its oxidized state from the aerobic CO utilizing bacteria Oligotropha carboxidovorans and Hydrogenophaga pseudoflava.
X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution.
A three-dimensional structure for the monomeric iron-containing hydrogenase (CpI) from Clostridium pasteurianum was determined, providing insights into the mechanism of biological hydrogen activation and has broader implications for [Fe-S] cluster structure and function in biological systems.
A Multinuclear ENDOR Study of the C-Cluster in CO Dehydrogenase from Clostridium thermoaceticum: Evidence for HxO and Histidine Coordination to the [Fe4S4] Center
The C-cluster of carbon monoxide dehydrogenase (CODH) catalyzes the reversible oxidation of CO to form CO2. This study reports electron nuclear double resonance (ENDOR) spectroscopy of the
Sulfite Reductase Structure at 1.6 Å: Evolution and Catalysis for Reduction of Inorganic Anions
The crystallographic structure of Escherichia coli sulfite reductase hemoprotein (SiRHP), which catalyzes the concerted six-electron reductions of sulfite to sulfide and nitrite to ammonia, was solved with multiwavelength anomalous diffraction (MAD) of the native siroheme and Fe 4S4 cluster cofactors, multiple isomorphous replacement, and selenomethionine sequence markers.
Nickel-Containing Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase†,‡
This article reviews an enzyme with two important catalytic activities, carbon monoxide dehydrogenase (CODH) (reaction 1) and acetyl-CoA synthase (ACS) (reaction 2). These reactions are key to an
Nature of the C-Cluster in Ni-Containing Carbon Monoxide Dehydrogenases
The C-cluster of carbon monoxide dehydrogenase (CODH) appears to be the active site for the oxidation of CO to CO2. We have studied with EPR and Mossbauer spectroscopy the enzymes from Rhodospirill...
Iron-sulfur proteins: new roles for old clusters.
  • M. Johnson
  • Chemistry
    Current opinion in chemical biology
  • 1998
The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase.
The structure of the catalytically inactive Mo(minus) CODH indicates that an intracellular Mo-deficiency affects exclusively the active site of the enzyme as an incomplete non-functional molybdenum cofactor was synthesized.