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

Yoshihide Tokunou; Punthira Chinotaikul; Shingo Hattori; Thomas A Clarke; Liang Shi; Kazuhito Hashimoto; Kazuyuki Ishii; Akihiro Okamoto

doi:10.1039/c8cc06309e

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

Chem Commun (Camb). 2018 Dec 11;54(99):13933-13936. doi: 10.1039/c8cc06309e.

Authors

Yoshihide Tokunou¹, Punthira Chinotaikul, Shingo Hattori, Thomas A Clarke, Liang Shi, Kazuhito Hashimoto, Kazuyuki Ishii, Akihiro Okamoto

Affiliation

¹ Department of Applied Chemistry, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.

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.

MeSH terms

Bacterial Outer Membrane Proteins / chemistry*
Bacterial Proteins / chemistry*
Circular Dichroism / methods*
Cytochromes / chemistry*
Electron Transport
Heme / chemistry*
Kinetics
Oxidation-Reduction
Protein Conformation
Shewanella / enzymology*
Spectrum Analysis / methods*

Substances

Bacterial Outer Membrane Proteins
Bacterial Proteins
Cytochromes
MtrB protein, Shewanella putrefaciens
Heme