Open AccessNifB-dependent in vitro synthesis of the iron–molybdenum cofactor of nitrogenase
Author(s) -
Leonardo Curatti,
Paul W. Ludden,
Luis M. Rubio
Publication year - 2006
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.0601115103
Subject(s) - nitrogenase , cofactor , molybdenum , chemistry , nitrogen fixation , in vitro , azotobacter vinelandii , biogeochemical cycle , enzyme , stereochemistry , biochemistry , nitrogen , combinatorial chemistry , inorganic chemistry , organic chemistry
Biological nitrogen fixation, an essential process of the biogeochemical nitrogen cycle that supports life on Earth, is catalyzed by the nitrogenase enzyme. The nitrogenase active site contains an iron and molybdenum cofactor (FeMo-co) composed of 7Fe-9S-Mo-homocitrate and one not-yet-identified atom, which probably is the most complex [Fe–S] cluster in nature. Here, we show thein vitro synthesis of FeMo-co from its simple constituents, Fe, S, Mo, and homocitrate. Thein vitro FeMo-co synthesis requires purified NifB and depends onS -adenosylmethionine, indicating that radical chemistry is required during FeMo-co assembly.