title: Refining the pathway of carbide insertion into the nitrogenase M-cluster.
abstract: Carbide insertion plays a pivotal role in the biosynthesis of M-cluster, the cofactor of nitrogenase. Previously, we proposed a carbide insertion pathway involving methyltransfer from SAM to a FeS precursor and hydrogen abstraction from this methyl group that initiates the radical-based precursor maturation. Here we demonstrate that the methyl group is transferred to a precursor-associated sulfur before hydrogen abstraction, thereby refining the initial steps of the carbide insertion pathway.
authors.affiliation: Department of Molecular Biology and Biochemistry, University of California, Irvine, California 92697-3900, USA.
authors.forename: Jared A
authors.initials: JA
authors.lastname: Wiig
authors.affiliation: Department of Molecular Biology and Biochemistry, University of California, Irvine, California 92697-3900, USA.
authors.forename: Yilin
authors.initials: Y
authors.lastname: Hu
authors.affiliation: Department of Molecular Biology and Biochemistry, University of California, Irvine, California 92697-3900, USA.|Department of Chemistry, University of California, Irvine, California 92697-2025, USA.
authors.forename: Markus W
authors.initials: MW
authors.lastname: Ribbe
mesh_terms: D016948:Azotobacter vinelandii / Q000502:physiology; D001426:Bacterial Proteins; D003067:Coenzymes / Q000737:chemistry / Q000502:physiology*; D008958:Models, Molecular; D015394:Molecular Structure; D009591:Nitrogenase / Q000378:metabolism*; D011487:Protein Conformation; D064586:Selenic Acid
chemical_list: D001426:Bacterial Proteins; D003067:Coenzymes; D009591:Nitrogenase; D064586:Selenic Acid