Sequence and electron paramagnetic resonance analyses of nitrate reductase NarGH from a denitrifying halophilic euryarchaeote Haloarcula marismortui

FEBS Lett. 2002 Apr 10;516(1-3):145-50. doi: 10.1016/s0014-5793(02)02524-3.


Genes encoding the NarG and NarH subunits of the molybdo-iron-sulfur enzyme, a nitrate reductase from a denitrifying halophilic euryarchaeota Haloarcula marismortui, were cloned and sequenced. An incomplete cysteine motif reminiscent of that for a [4Fe-4S] cluster binding was found in the NarG subunit, and complete cysteine arrangements for binding one [3Fe-4S] cluster and three [4Fe-4S] clusters were found in the NarH subunit. In conjunction with chemical, electron paramagnetic resonance, and subcellular localization analyses, we firmly establish that the H. marismortui enzyme is a new archaeal member of the known membrane-bound nitrate reductases whose homologs are found in the bacterial domain.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Cloning, Molecular
  • DNA, Archaeal / genetics
  • Electron Spin Resonance Spectroscopy
  • Genes, Archaeal
  • Genes, Bacterial
  • Haloarcula marismortui / enzymology*
  • Haloarcula marismortui / genetics*
  • Molecular Sequence Data
  • Nitrate Reductase
  • Nitrate Reductases / chemistry*
  • Nitrate Reductases / genetics*
  • Protein Subunits
  • Sequence Homology, Amino Acid
  • Subcellular Fractions / enzymology


  • DNA, Archaeal
  • Protein Subunits
  • Nitrate Reductases
  • Nitrate Reductase

Associated data

  • GENBANK/AJ429077