Biosynthesis of the iron-molybdenum cofactor of nitrogenase.
The iron-molybdenum cofactor (FeMo-co), located at the active site of the molybdenum nitrogenase, is one of the most complex metal cofactors known to date. During the past several years, an intensive effort has been made to purify the proteins involved in FeMo-co synthesis and incorporation into nitrogenase. This effort is starting to provide insights into the structures of the FeMo-co biosynthetic intermediates and into the biochemical details of FeMo-co synthesis.
Rubio
Luis M
LM
Department of Plant and Microbial Biology, University of California, Berkeley, California 94720, USA. lrubio@nature.berkeley.edu
Ludden
Paul W
PW
D000595:Amino Acid Sequence; D001419:Bacteria / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D020134:Catalytic Domain; D005798:Genes, Bacterial; D008954:Models, Biological; D008958:Models, Molecular; D008982:Molybdenum / Q000378:metabolism; D008983:Molybdoferredoxin / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D005810:Multigene Family; D009586:Nitrogen Fixation / Q000235:genetics / Q000502:physiology; D009591:Nitrogenase / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D020836:Protein Structure, Quaternary; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D008983:Molybdoferredoxin; D008982:Molybdenum; D009591:Nitrogenase