title: Iron-molybdenum cofactor synthesis in Azotobacter vinelandii Nif- mutants.
abstract: Nif- mutants of Azotobacter vinelandii defective in dinitrogenase activity synthesized iron-molybdenum cofactor (FeMo-co) and accumulated it in two protein-bound forms: inactive dinitrogenase and a possible intermediate involved in the FeMo-co biosynthetic pathway. FeMo-co from both these proteins could activate apo-dinitrogenase from FeMo-co-deficient mutants.
authors.forename: J
authors.initials: J
authors.lastname: Imperial
authors.forename: V K
authors.initials: VK
authors.lastname: Shah
authors.forename: R A
authors.initials: RA
authors.lastname: Ugalde
authors.forename: P W
authors.initials: PW
authors.lastname: Ludden
authors.forename: W J
authors.initials: WJ
authors.lastname: Brill
mesh_terms: D001395:Azotobacter / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D005288:Ferredoxins / Q000096:biosynthesis*; D008983:Molybdoferredoxin / Q000096:biosynthesis* / Q000378:metabolism; D009154:Mutation; D009591:Nitrogenase / Q000235:genetics / Q000378:metabolism*; D010088:Oxidoreductases
chemical_list: D005288:Ferredoxins; D008983:Molybdoferredoxin; D010088:Oxidoreductases; D009591:Nitrogenase; C029130:nitrogenase reductase