9-Mercaptodethiobiotin is generated as a ligand to the [2Fe-2S]+ cluster during the reaction catalyzed by biotin synthase from Escherichia coli.

@article{Fugate20129MercaptodethiobiotinIG,
  title={9-Mercaptodethiobiotin is generated as a ligand to the [2Fe-2S]+ cluster during the reaction catalyzed by biotin synthase from Escherichia coli.},
  author={Corey J. Fugate and Troy A Stich and Esther Grace Kim and William K Myers and R David Britt and Joseph T Jarrett},
  journal={Journal of the American Chemical Society},
  year={2012},
  volume={134 22},
  pages={
          9042-5
        }
}
Biotin synthase catalyzes formation of the thiophane ring through stepwise substitution of a sulfur atom for hydrogen atoms at the C9 and C6 positions of dethiobiotin. Biotin synthase is a radical S-adenosylmethionine (SAM) enzyme that reductively cleaves S-adenosylmethionine, generating 5'-deoxyadenosyl radicals that initially abstract a hydrogen atom from the C9 position of dethiobiotin. We have proposed that the resulting dethiobiotinyl radical is quenched by the μ-sulfide of the nearby [2Fe… CONTINUE READING

References

Publications referenced by this paper.

The non-heme iron enzyme, isopenicillin-N-synthase, is a rare example of a metal-oxygen system that can form a C−S

M. Fontecave, S. Ollagnier-de-Choudens, E. Chem. Rev. Mulliez
  • Curr. Opin. Chem. Biol
  • 2003