EPR evidence for a fast-relaxing iron center in Na+-translocating NADH: quinone-oxidoreductase

Leonid V. Kulik, Yulia V. Bertsova, Alexander V. Bogachev

Research output: Contribution to journalArticlepeer-review


A paramagnetic Cys4[Fe] center was detected by pulse EPR in Na+-translocating NADH:quinone-oxidoreductase (Na+-NQR) by influence of this center on transverse and longitudinal spin relaxation of Na+-NQR flavin radicals. The oxidation state of the Cys4[Fe] center was Fe3+ in the oxidized and Fe2+ in the reduced Na+-NQR, as deduced from the temperature dependence of spin relaxation rates of different flavin radicals. A high-spin state of iron in the Cys4[Fe] center was assigned to both forms of Na+-NQR.

Original languageEnglish
Pages (from-to)15-18
Number of pages4
JournalJournal of Inorganic Biochemistry
Publication statusPublished - 1 Jul 2018


  • Electron paramagnetic resonance
  • Flavin radicals
  • Mononuclear iron center
  • NADH:quinone oxidoreductase
  • Spin relaxation
  • Electron Spin Resonance Spectroscopy/methods
  • Temperature
  • Oxidation-Reduction
  • Bacterial Proteins/chemistry
  • NAD(P)H Dehydrogenase (Quinone)/chemistry
  • Iron/chemistry


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