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- W2084813215 endingPage "3994" @default.
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- W2084813215 abstract "Nitrogenase, [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." @default.
- W2084813215 created "2016-06-24" @default.
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- W2084813215 creator A5059249230 @default.
- W2084813215 creator A5073568934 @default.
- W2084813215 creator A5076659724 @default.
- W2084813215 date "2015-02-01" @default.
- W2084813215 modified "2023-10-13" @default.
- W2084813215 title "Radical S-Adenosyl-l-methionine Chemistry in the Synthesis of Hydrogenase and Nitrogenase Metal Cofactors" @default.
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- W2084813215 doi "https://doi.org/10.1074/jbc.r114.578161" @default.
- W2084813215 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4326809" @default.
- W2084813215 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25477518" @default.
- W2084813215 hasPublicationYear "2015" @default.
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