A Ni-Fe-Cu Center in a Bifunctional Carbon Monoxide Dehydrogenase/ Acetyl-CoA Synthase

@article{Doukov2002ANC,
  title={A Ni-Fe-Cu Center in a Bifunctional Carbon Monoxide Dehydrogenase/ Acetyl-CoA Synthase},
  author={Tzanko I. Doukov and Tina M Iverson and Javier Seravalli and Stephen W. Ragsdale and Catherine L. Drennan},
  journal={Science},
  year={2002},
  volume={298},
  pages={567 - 572}
}
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 (f.Clostridium thermoaceticum). Our structure at 2.2 angstrom resolution reveals that the cofactor responsible for the assembly of acetyl-CoA contains a [Fe4S4] cubane bridged to a copper-nickel binuclear site. The presence of these three metals together in one cluster was unanticipated and suggests a newly… 
Acetyl-coenzyme A synthase: the case for a Nip0-based mechanism of catalysis
  • P. Lindahl
  • Chemistry
    JBIC Journal of Biological Inorganic Chemistry
  • 2004
TLDR
In this review, evidence is presented that Nip achieves a zero-valent state at low potentials and during catalysis, and Ni-organometallic complexes in which the Ni exhibits analogous reactivity properties when reduced to the zero-Valent state are reinforced.
Crystallographic Characterization of the Carbonylated A-Cluster in Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase
TLDR
Direct structural characterization of CODH/ACS from Moorella thermoacetica with substrate carbon monoxide bound at the A-cluster highlights the role of second sphere residues and conformational dynamics in acetyl-CoA assembly, the biological equivalent of the Monsanto process.
Nickel in subunit beta of the acetyl-CoA decarbonylase/synthase multienzyme complex in methanogens. Catalytic properties and evidence for a binuclear Ni-Ni site.
TLDR
A mechanism for C-C bond activation is proposed that includes a specific role for the Fe(4)S( 4) center and accounts for the absolute requirement for nickel.
CO Dehydrogenase/Acetyl‐CoA Synthase
TLDR
The bifunctional tetrameric enzyme carbon monoxide dehydrogenase (CODH)/acetyl-CoA synthase (ACS) undergoes a conformational change that blocks the tunnel near the active site, preventing the escape of the toxic CO from within the enzyme upon methyl binding to nickel.
Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase
TLDR
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.
Different modes of carbon monoxide binding to acetyl-CoA synthase and the role of a conserved phenylalanine in the coordination environment of nickel.
TLDR
A model was developed for how the catalytic properties of the A cluster are optimized by linking conformational changes to a repositionable aromatic shield able to modulate the nucleophilicity of Ni, sterically select the most productive order of substrate addition, and overcome intrinsic inhibition by CO.
Functional copper at the acetyl-CoA synthase active site
TLDR
Evidence is presented that the copper ion at the M. thermoacetica ACS active site is essential and an essential and functional role for copper in the CODH/ACS from acetogenic and methanogenic organisms.
Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open α subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase
TLDR
It is postulate that only the A-clusters containing two Ni ions are catalytically active in the tetrameric α2β2 acetyl-coenzyme A synthase/carbon monoxide dehydrogenase from Moorella thermoacetica.
Targeting synthetic analogues of the metallo-sulfur active sites of nickel enzymes capable of important catalysis
The nickel containing enzymes NiFe-hydrogenase, carbon monoxide dehydrogenase and acetyl-CoA synthase are able to catalyse environmentally, and potentially industrially, important reactions: hydrogen
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TLDR
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.
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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
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TLDR
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