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A radical solution for the biosynthesis of the H‐cluster of hydrogenase
Author(s) -
Peters John W.,
Szilagyi Robert K.,
Naumov Anatoli,
Douglas Trevor
Publication year - 2006
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.2005.12.040
Subject(s) - hydrogenase , biosynthesis , chemistry , cluster (spacecraft) , biochemistry , gene cluster , photochemistry , enzyme , computer science , gene , programming language
Fe‐only or FeFe hydrogenases, as they have more recently been termed, possess a uniquely organometallic enzyme active site, termed the H‐cluster, where the electronic properties of an iron–sulfur cluster are tuned with distinctly non‐biological ligands, carbon monoxide and cyanide. Recently, it was discovered that radical S ‐adenosylmethionine enzymes were involved in active hydrogenase expression. In the current work, we present a mechanistic scheme for hydrogenase H‐cluster biosynthesis in which both carbon monoxide and cyanide ligands can be derived from the decomposition of a glycine radical. The ideas presented have broader implications in the context of the prebiotic origin of amino acids.