Crystallographic analysis of the MoFe protein of nitrogenase from a nifV mutant of Klebsiella pneumoniae identifies citrate as a ligand to the molybdenum of iron molybdenum cofactor (FeMoco)

J Biol Chem. 2002 Sep 20;277(38):35263-6. doi: 10.1074/jbc.M205888200. Epub 2002 Jul 19.

Abstract

The x-ray crystal structure of NifV(-) Klebsiella pneumoniae nitrogenase MoFe protein (NifV(-) Kp1) has been determined and refined to a resolution of 1.9 A. This is the first structure for a nitrogenase MoFe protein with an altered cofactor. Moreover, it is the first direct evidence that the organic acid citrate is not just present, but replaces homocitrate as a ligand to the molybdenum atom of the iron molybdenum cofactor (FeMoco). Subsequent refinement of the structure revealed that the citrate was present at reduced occupancy.

MeSH terms

  • Citrates / metabolism*
  • Crystallography, X-Ray
  • Klebsiella pneumoniae / enzymology*
  • Klebsiella pneumoniae / genetics
  • Ligands
  • Models, Molecular
  • Molybdenum / metabolism*
  • Molybdoferredoxin / chemistry*
  • Molybdoferredoxin / metabolism*
  • Mutation*
  • Nitrogenase / chemistry*
  • Oxo-Acid-Lyases / genetics*
  • Protein Conformation

Substances

  • Citrates
  • Ligands
  • Molybdoferredoxin
  • Molybdenum
  • Nitrogenase
  • homocitrate synthase
  • Oxo-Acid-Lyases

Associated data

  • PDB/1H1L
  • PDB/1QGU
  • PDB/R1H1LSF