Characterization of the paramagnetic iron-containing redox centres of Thiosphaera pantotropha periplasmic nitrate reductase

Jacques Breton, Ben C. Berks, Ann Reilly, Andrew J. Thomson, Stuart J. Ferguson, David J. Richardson

Research output: Contribution to journalArticlepeer-review

56 Citations (Scopus)


Electron paramagnetic resonance spectroscopy signals attributable to low-spin haem c in the oxidised protein and [4Fe4S]1+ in the dithionite-reduced protein were identified, at low temperature, in Thiosphaera pantotropha periplasmic nitrate reductase. Spin integration of these signals as well as elemental analysis suggest a stoichiometry of 1.3-1.6 c-haem and 1 [4Fe4S] cluster per enzyme molecule. The Em (at pH 7.4) of the [4F4S]2+,1+ couple, -160 mV, means that it is unlikely to be physiologically reducible. Peptide sequences from the 90 kDa subunit indicate that the enzyme is a member of the family of molybdopterin guanine dinucleotide-binding polypeptides, the majority of which possess a putative [4Fe4S] cluster binding sequence and thus may also bind a (low potential) iron-sulphur cluster.

Original languageEnglish
Pages (from-to)76-80
Number of pages5
JournalFEBS Letters
Issue number1
Publication statusPublished - 23 May 1994


  • cytochrome c-type
  • Iron-sulphur protein
  • Periplasmic nitrate reductase
  • Thiosphaera pantotropha

Cite this