Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2052021 | FEBS Letters | 2006 | 5 Pages |
Abstract
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.
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Authors
John W. Peters, Robert K. Szilagyi, Anatoli Naumov, Trevor Douglas,