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Keywords:

  • Enzymes;
  • [FeFe]-Hydrogenase;
  • Carbon monoxide;
  • Cyanide;
  • Active site maturation

Abstract

Recent work conducted in several laboratories has shown that the [FeFe]-hydrogenase maturase HydG synthesizes both CO and CN from tyrosine. We have very recently found that although CN synthesis does not need the [4Fe-4S] cluster found in the HydG C-terminal domain, CO synthesis does require it. We have also proposed that the +H2N·–CH2–CO2 radical is a precursor for these two active site ligands. Here, we have extended our characterization of both the wild-type enzyme and a ThiH-like HydG truncated mutant, with small angle X-ray scattering (SAXS) spectroscopy, homology modeling and functional studies.