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

Publisher Website
Google Scholar
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.