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The role of the maturase HydG in [FeFe]‐hydrogenase active site synthesis and assembly
Author(s) -
Pilet Eric,
Nicolet Yvain,
Mathevon Carole,
Douki Thierry,
Fontecilla-Camps Juan C.,
Fontecave Marc
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.01.004
Subject(s) - active site , chemistry , hydrogenase , tyrosine , stereochemistry , ligand (biochemistry) , enzyme , iron–sulfur cluster , sulfur , crystallography , photochemistry , biochemistry , receptor , organic chemistry
[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 cleavage reaction catalyzed by HydG suggests a mechanism for hydrogenase maturation. Here we propose that HydG is specifically involved in the synthesis of the dithiolate ligand, with two tyrosine‐derived dehydroglycines as precursors along with an [FeS] cluster of HydG functioning both as electron shuttle and source of the sulfur atoms.