Unraveling the structure and mechanism of acetyl-coenzyme A synthase.

@article{Hegg2004UnravelingTS,
  title={Unraveling the structure and mechanism of acetyl-coenzyme A synthase.},
  author={Eric L. Hegg},
  journal={Accounts of chemical research},
  year={2004},
  volume={37 10},
  pages={
          775-83
        }
}
  • E. Hegg
  • Published 18 August 2004
  • Chemistry
  • Accounts of chemical research
The bifunctional enzyme carbon monoxide dehydrogenase/acetyl-coenzyme A (CoA) synthase (CODH/ACS) is a key enzyme in the Wood-Ljungdahl pathway of carbon fixation. Carbon monoxide is combined with a methyl group and ultimately converted to acetyl-CoA at a unique Ni-containing bimetallic site in the A-cluster of this enzyme. Despite years of extensive biochemical and spectroscopic studies and the recent report of three separate crystal structures, the mechanism by which acetyl-CoA is synthesized… 

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TLDR
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The conversion of nickel-bound CO into an acetyl thioester: organometallic chemistry relevant to the acetyl coenzyme A synthase active site.
TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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