Biosynthesis of the iron-molybdenum cofactor of nitrogenase

Annu Rev Microbiol. 2008:62:93-111. doi: 10.1146/annurev.micro.62.081307.162737.

Abstract

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Amino Acid Sequence
  • Bacteria / genetics
  • Bacteria / metabolism*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Catalytic Domain
  • Genes, Bacterial
  • Models, Biological
  • Models, Molecular
  • Molybdenum / metabolism
  • Molybdoferredoxin / biosynthesis*
  • Molybdoferredoxin / chemistry
  • Molybdoferredoxin / genetics
  • Multigene Family
  • Nitrogen Fixation / genetics
  • Nitrogen Fixation / physiology
  • Nitrogenase / biosynthesis*
  • Nitrogenase / chemistry
  • Nitrogenase / genetics
  • Protein Structure, Quaternary
  • Sequence Homology, Amino Acid

Substances

  • Bacterial Proteins
  • Molybdoferredoxin
  • Molybdenum
  • Nitrogenase