Byer, Amanda S.Shepard, Eric M.Peters, John W.Broderick, Joan B.2015-07-132015-07-132014-12Byer, Amanda S., Eric M. Shepard, John W. Peters, and Joan B. Broderick. Radical S -Adenosyl-l-Methionine Chemistry in the Synthesis of Hydrogenase and Nitrogenase Metal Cofactors. J. Biol. Chem. 290, no. 7 (December 4, 2014): 3987-3994. doi:10.1074/jbc.r114.578161.0021-9258https://scholarworks.montana.edu/handle/1/9184Nitrogenase, [FeFe]-hydrogenase, and [Fe]-hydrogenase enzymes perform catalysis at metal cofactors with biologically unusual non-protein ligands. The FeMo cofactor of nitrogenase has a MoFe7S9 cluster with a central carbon, whereas the H-cluster of [FeFe]-hydrogenase contains a 2Fe subcluster coordinated by cyanide and CO ligands as well as dithiomethylamine; the [Fe]-hydrogenase cofactor has CO and guanylylpyridinol ligands at a mononuclear iron site. Intriguingly, radical S-adenosyl-L-methionine enzymes are vital for the assembly of all three of these diverse cofactors. This minireview presents and discusses the current state of knowledge of the radical S-adenosylmethionine enzymes required for synthesis of these remarkable metal cofactors.HydrogenaseInorganic chemistryArticle