title: Nucleotide and divalent cation specificity of in vitro iron-molybdenum cofactor synthesis.
abstract: The nucleotide and divalent cation requirements of the in vitro iron-molybdenum cofactor (FeMo-co) synthesis system have been compared with those of substrate reduction by nitrogenase. The FeMo-co synthesis system specifically requires ATP, whereas both 1,N6-etheno-ATP and 2'-deoxy-ATP function in place of ATP in substrate reduction (M. F. Weston, S. Kotake, and L. C. Davis, Arch. Biochem. Biophys. 225:809-817, 1983). Mn2+, Ca2+, and Fe2+ substitute for Mg2+ to various extents in in vitro FeMo-co synthesis, whereas Ca2+ is ineffective in substrate reduction by nitrogenase. The observed differences in the nucleotide and divalent cation specificities suggest a role(s) for the nucleotide and divalent cation in in vitro FeMo-co synthesis that is distinct from their role(s) in substrate reduction.
authors.affiliation: Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin-Madison 53706.
authors.forename: R
authors.initials: R
authors.lastname: Chatterjee
authors.forename: R M
authors.initials: RM
authors.lastname: Allen
authors.forename: V K
authors.initials: VK
authors.lastname: Shah
authors.forename: P W
authors.initials: PW
authors.lastname: Ludden
mesh_terms: D000255:Adenosine Triphosphate / Q000031:analogs & derivatives; D001051:Apoenzymes / Q000378:metabolism; D016948:Azotobacter vinelandii / Q000201:enzymology / Q000378:metabolism*; D002413:Cations, Divalent / Q000494:pharmacology; D003035:Cobalt / Q000378:metabolism; D005030:Ethylenes / Q000378:metabolism; D008983:Molybdoferredoxin / Q000096:biosynthesis*; D009591:Nitrogenase / Q000378:metabolism; D009711:Nucleotides / Q000494:pharmacology
chemical_list: D001051:Apoenzymes; D002413:Cations, Divalent; D005030:Ethylenes; D008983:Molybdoferredoxin; D009711:Nucleotides; D003035:Cobalt; D000255:Adenosine Triphosphate; C036216:ethylene; D009591:Nitrogenase