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

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.

SUBMITTER: Tokunou Y

PROVIDER: S-EPMC6301274 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature

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

Tokunou Yoshihide Y Chinotaikul Punthira P Hattori Shingo S Clarke Thomas A TA Shi Liang L Hashimoto Kazuhito K Ishii Kazuyuki K Okamoto Akihiro A

Chemical communications (Cambridge, England) 20181201 99

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. ...[more]

PMID: 30403202

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