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Octaheme tetrathionate reductase is a respiratory enzyme with novel heme ligation

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 ε-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.

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Figure 1: Structure of octaheme tetrathionate reductase.
Figure 2: Heme arrangement in octaheme tetrathionate reductase.

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Acknowledgements

We thank the UK Biotechnology and Biological Sciences Research Council for grant funding to G.A.R. and S.K.C. and the Wellcome Trust for their support to the Edinburgh Protein Interaction Centre. Synchrotron access at European Molecular Biology Laboratory Hamburg was supported by the European Commission (contract HPRI-CT-1999-00017).

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Correspondence to Graeme A Reid.

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The authors declare no competing financial interests.

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Supplementary Table

Data collection, phasing and refinement statistics for OTR (PDF 18 kb)

Supplementary Methods (PDF 34 kb)

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Mowat, C., Rothery, E., Miles, C. et al. Octaheme tetrathionate reductase is a respiratory enzyme with novel heme ligation. Nat Struct Mol Biol 11, 1023–1024 (2004). https://doi.org/10.1038/nsmb827

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