title: FeMo cofactor maturation on NifEN.
abstract: FeMo cofactor (FeMoco) biosynthesis is one of the most complicated processes in metalloprotein biochemistry. Here we show that Mo and homocitrate are incorporated into the Fe/S core of the FeMoco precursor while it is bound to NifEN and that the resulting fully complemented, FeMoco-like cluster is transformed into a mature FeMoco upon transfer from NifEN to MoFe protein through direct protein-protein interaction. Our findings not only clarify the process of FeMoco maturation, but also provide useful insights into the other facets of nitrogenase chemistry.
authors.affiliation: Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, USA.
authors.forename: Yilin
authors.initials: Y
authors.lastname: Hu
authors.forename: Mary C
authors.initials: MC
authors.lastname: Corbett
authors.forename: Aaron W
authors.initials: AW
authors.lastname: Fay
authors.forename: Jerome A
authors.initials: JA
authors.lastname: Webber
authors.forename: Keith O
authors.initials: KO
authors.lastname: Hodgson
authors.forename: Britt
authors.initials: B
authors.lastname: Hedman
authors.forename: Markus W
authors.initials: MW
authors.lastname: Ribbe
mesh_terms: D004578:Electron Spin Resonance Spectroscopy; D008983:Molybdoferredoxin / Q000737:chemistry* / Q000378:metabolism*; D009586:Nitrogen Fixation; D009591:Nitrogenase / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D008983:Molybdoferredoxin; D009591:Nitrogenase