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Whole-cell circular dichroism difference spectroscopy reveals an in vivo-specific deca-heme conformation in bacterial surface cytochromes

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Abstract

We established whole-cell circular dichroism difference spectroscopy to identify the inter-heme interaction in deca-heme cytochrome protein MtrC in whole cell. Our data showed that the heme alignment of reduced MtrC in whole cell is distinct from that in purified one, suggesting the in vivo specific electron transport kinetics.

Graphical abstract: Whole-cell circular dichroism difference spectroscopy reveals an in vivo-specific deca-heme conformation in bacterial surface cytochromes

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Publication details

The article was received on 02 Aug 2018, accepted on 12 Sep 2018 and first published on 07 Nov 2018


Article type: Communication
DOI: 10.1039/C8CC06309E
Citation: Chem. Commun., 2018, Advance Article
  • Open access: Creative Commons BY license
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    Whole-cell circular dichroism difference spectroscopy reveals an in vivo-specific deca-heme conformation in bacterial surface cytochromes

    Y. Tokunou, P. Chinotaikul, S. Hattori, T. A. Clarke, L. Shi, K. Hashimoto, K. Ishii and A. Okamoto, Chem. Commun., 2018, Advance Article , DOI: 10.1039/C8CC06309E

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