EXAFS reveals two Mo environments in the nitrogenase iron-molybdenum cofactor biosynthetic protein NifQ

Chem Commun (Camb). 2016 Sep 27;52(79):11811-11814. doi: 10.1039/c6cc06370e.

Abstract

Mo and Fe K-edge EXAFS analysis of NifQ shows the presence of a [MoFe3S4] cluster and a second independent Mo environment that includes Mo-O bonds and Mo-S bonds. Both environments are relevant to FeMo-co biosynthesis and may represent different stages of Mo biochemical transformations catalyzed by NifQ.

MeSH terms

  • 2,2'-Dipyridyl / chemistry
  • Azotobacter vinelandii / enzymology
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Coenzymes / chemistry*
  • Copper / chemistry
  • Iron / chemistry
  • Metalloproteins / chemistry*
  • Molybdenum Cofactors
  • Nitrogenase / metabolism*
  • Pteridines / chemistry*
  • Transcription Factors / chemistry
  • Transcription Factors / metabolism*
  • X-Ray Absorption Spectroscopy

Substances

  • Bacterial Proteins
  • Coenzymes
  • Metalloproteins
  • Molybdenum Cofactors
  • NifQ protein, Azotobacter vinelandii
  • Pteridines
  • Transcription Factors
  • 2,2'-Dipyridyl
  • Copper
  • molybdenum cofactor
  • Iron
  • Nitrogenase
  • cupric chloride