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Related Experiment Videos

Functional copper at the acetyl-CoA synthase active site.

Javier Seravalli1, Weiwei Gu, Annie Tam

  • 1Department of Biochemistry, University of Nebraska, Lincoln, NE 68588, USA.

Proceedings of the National Academy of Sciences of the United States of America
|February 18, 2003
PubMed
Summary

Copper is essential for the activity of acetyl-CoA synthase (ACS) in the Wood-Ljungdahl pathway. This study provides evidence for copper

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Area of Science:

  • Biochemistry
  • Bioinorganic Chemistry
  • Enzymology

Background:

  • The bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS) is crucial for autotrophic CO2 fixation via the Wood-Ljungdahl pathway.
  • Structural studies revealed a binuclear copper-nickel (Cu-Ni) site within the ACS active site.

Purpose of the Study:

  • To investigate the essential role of copper in the active site of CODH/ACS from Moorella thermoacetica.
  • To elucidate the function of copper in the catalytic mechanism of acetyl-CoA synthesis.

Main Methods:

  • Biochemical assays to measure enzyme activity.
  • X-ray absorption spectroscopy (XAS) including extended X-ray absorption fine structure (EXAFS) and X-ray absorption near-edge structure (XANES).
  • Electron paramagnetic resonance (EPR) spectroscopy.

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Main Results:

  • Copper depletion significantly reduced ACS activity and altered the EPR signal of the NiFeC cluster, while CODH activity remained unaffected.
  • Zinc content showed a negative correlation with ACS activity.
  • XAS studies indicated a distorted Cu(I)-S3 site in the active enzyme and a Cu-S3Se environment upon seleno-CoA binding, suggesting a Cu-SCoA intermediate.

Conclusions:

  • Copper is an essential component of the ACS active site in both acetogenic (M. thermoacetica) and methanogenic (M. thermophila) organisms.
  • The findings implicate copper in the catalytic mechanism of acetyl-CoA synthesis, likely through a copper-thioester intermediate.