The role of the maturase HydG in [FeFe]-hydrogenase active site synthesis and assembly.

@article{Pilet2009TheRO,
  title={The role of the maturase HydG in [FeFe]-hydrogenase active site synthesis and assembly.},
  author={Eric Pilet and Yvain Nicolet and Carole Mathevon and Thierry Douki and Juan C Fontecilla-Camps and Marc Fontecave},
  journal={FEBS letters},
  year={2009},
  volume={583 3},
  pages={506-11}
}
[FeFe]-hydrogenases catalyze the protons/hydrogen interconversion through a unique di-iron active site consisting of three CO and two CN ligands, and a non-protein SCH(2)XCH(2)S (X=N or O) dithiolate bridge. Site assembly requires two "Radical-S-adenosylmethionine (SAM or AdoMet)" iron-sulfur enzymes, HydE and HydG, and one GTPase, HydF. The sequence homology between HydG and ThiH, a Radical-SAM enzyme which cleaves tyrosine into p-cresol and dehydroglycine, and the finding of a similar… CONTINUE READING

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