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

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    Abstract

    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 and Molecular Biology
    Volume11
    Issue number10
    DOIs
    Publication statusPublished - 2004

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    Mowat, C. G., Rothery, E., Miles, C. S., McIver, L., Doherty, M. K., Drewette, K., Taylor, P., Walkinshaw, M. D., Chapman, S. K., & Reid, G. A. (2004). Octaheme tetrathionate reductase is a respiratory enzyme with novel heme ligation. Nature Structural and Molecular Biology, 11(10), 1023-1024. https://doi.org/10.1038/nsmb827