title: Crystallographic structure and functional implications of the nitrogenase molybdenum-iron protein from azotobacter vinelandii.
abstract: The crystal structure of the nitrogenase molybdenum–iron protein from Azotobacter vinelandii has been determined at 2.7 Å resolution. The α- and β-subunits in this α (2) β (2) tetramer have similar polypeptide folds. The FeMo-cofactor is completely encompassed by the α-subunit, whereas the P-cluster pair occurs at the interface between α- and β-subunits. Structural similarities are apparent between nitrogenase and other electron transfer systems, including hydrogenases and the photosynthetic reaction centre
authors.affiliation: Division of Chemistry and Chemical Engineering 147-75CH, California Institute of Technology, Pasadena, California 91125, USA.
authors.forename: J
authors.initials: J
authors.lastname: Kim
authors.forename: D C
authors.initials: DC
authors.lastname: Rees