Sequence and electron paramagnetic resonance analyses of nitrate reductase NarGH from a denitrifying halophilic euryarchaeote Haloarcula marismortui.
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.
Yoshimatsu
Katsuhiko
K
Department of Biology and Geosciences, Faculty of Science, Shizuoka University, 836 Ohya, 422-8529, Shizuoka, Japan.
Iwasaki
Toshio
T
Fujiwara
Taketomo
T
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D019641:DNA, Archaeal / Q000235:genetics; D004578:Electron Spin Resonance Spectroscopy; D019766:Genes, Archaeal; D005798:Genes, Bacterial; D019614:Haloarcula marismortui / Q000201:enzymology* / Q000235:genetics*; D008969:Molecular Sequence Data; D050901:Nitrate Reductase; D009565:Nitrate Reductases / Q000737:chemistry* / Q000235:genetics*; D021122:Protein Subunits; D017386:Sequence Homology, Amino Acid; D013347:Subcellular Fractions / Q000201:enzymology
D019641:DNA, Archaeal; D021122:Protein Subunits; D009565:Nitrate Reductases; D050901:Nitrate Reductase