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Review
. 2006 Jan 23;580(2):363-7.
doi: 10.1016/j.febslet.2005.12.040. Epub 2005 Dec 22.

A radical solution for the biosynthesis of the H-cluster of hydrogenase

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Free article
Review

A radical solution for the biosynthesis of the H-cluster of hydrogenase

John W Peters et al. FEBS Lett. .
Free article

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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