A radical solution for the biosynthesis of the H-cluster of hydrogenase.
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.
Peters
John W
JW
Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59717, USA. john.peters@chemistry.montana.edu
Szilagyi
Robert K
RK
Naumov
Anatoli
A
Douglas
Trevor
T
D001665:Binding Sites; D002248:Carbon Monoxide / Q000378:metabolism; D003486:Cyanides / Q000378:metabolism; D005998:Glycine / Q000737:chemistry / Q000378:metabolism; D006864:Hydrogenase / Q000737:chemistry* / Q000378:metabolism; D008024:Ligands; D008958:Models, Molecular; D011487:Protein Conformation
D003486:Cyanides; D008024:Ligands; D002248:Carbon Monoxide; D006864:Hydrogenase; D005998:Glycine