Octaheme tetrathionate reductase is a respiratory enzyme with novel heme ligation

Christopher G Mowat, Emma Rothery, Caroline S Miles, Lisa McIver, Mary K Doherty, Katy Drewette, Paul Taylor, Malcolm D Walkinshaw, Stephen K Chapman, Graeme A Reid

Research output: Contribution to journalArticlepeer-review

85 Citations (Scopus)


We have isolated a soluble cytochrome from Shewanella oneidensis that contains eight covalently attached heme groups and determined its crystal structure. One of these hemes exhibits novel ligation of the iron atom by the epsilon-amino group of a lysine residue, despite its attachment via a typical CXXCH motif. This heme is most likely the active site for tetrathionate reduction, a reaction catalyzed efficiently by this enzyme.
Original languageEnglish
Pages (from-to)1023-1024
Number of pages2
JournalNature Structural & Molecular Biology
Issue number10
Publication statusPublished - Oct 2004


  • Binding Sites
  • Catalysis
  • Heme
  • Models, Molecular
  • Oxidoreductases
  • Protein Conformation
  • Shewanella


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