title: Radical AdoMet enzymes in complex metal cluster biosynthesis.
abstract: Radical S-adenosylmethionine (AdoMet) enzymes comprise a large superfamily of proteins that engage in a diverse series of biochemical transformations through generation of the highly reactive 5'-deoxyadenosyl radical intermediate. Recent advances into the biosynthesis of unique iron-sulfur (FeS)-containing cofactors such as the H-cluster in [FeFe]-hydrogenase, the FeMo-co in nitrogenase, as well as the iron-guanylylpyridinol (FeGP) cofactor in [Fe]-hydrogenase have implicated new roles for radical AdoMet enzymes in the biosynthesis of complex inorganic cofactors. Radical AdoMet enzymes in conjunction with scaffold proteins engage in modifying ubiquitous FeS precursors into unique clusters, through novel amino acid decomposition and sulfur insertion reactions. The ability of radical AdoMet enzymes to modify common metal centers to unusual metal cofactors may provide important clues into the stepwise evolution of these and other complex bioinorganic catalysts. This article is part of a Special Issue entitled: Radical SAM enzymes and Radical Enzymology.
authors.affiliation: The Department of Chemistry and Biochemistry and the Astrobiology Biogeocatalysis Research Center, Montana State University, Bozeman, MT 59717, USA.
authors.forename: Benjamin R
authors.initials: BR
authors.lastname: Duffus
authors.forename: Trinity L
authors.initials: TL
authors.lastname: Hamilton
authors.forename: Eric M
authors.initials: EM
authors.lastname: Shepard
authors.forename: Eric S
authors.initials: ES
authors.lastname: Boyd
authors.forename: John W
authors.initials: JW
authors.lastname: Peters
authors.forename: Joan B
authors.initials: JB
authors.lastname: Broderick
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D055162:Biocatalysis; D056831:Coordination Complexes / Q000737:chemistry / Q000378:metabolism; D019143:Evolution, Molecular; D005609:Free Radicals / Q000737:chemistry / Q000378:metabolism; D006864:Hydrogenase / Q000737:chemistry / Q000378:metabolism; D007501:Iron / Q000737:chemistry / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D008983:Molybdoferredoxin / Q000737:chemistry / Q000378:metabolism; D009591:Nitrogenase / Q000737:chemistry / Q000378:metabolism; D010802:Phylogeny; D012436:S-Adenosylmethionine / Q000737:chemistry / Q000378:metabolism*; D013455:Sulfur / Q000737:chemistry / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D056831:Coordination Complexes; D005609:Free Radicals; D007506:Iron-Sulfur Proteins; D008983:Molybdoferredoxin; D013455:Sulfur; D012436:S-Adenosylmethionine; D007501:Iron; C118830:iron hydrogenase; D006864:Hydrogenase; D009591:Nitrogenase