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

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...

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Autores principales: Tokunou, Yoshihide, Chinotaikul, Punthira, Hattori, Shingo, Clarke, Thomas A., Shi, Liang, Hashimoto, Kazuhito, Ishii, Kazuyuki, Okamoto, Akihiro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6301274/
https://www.ncbi.nlm.nih.gov/pubmed/30403202
http://dx.doi.org/10.1039/c8cc06309e
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author Tokunou, Yoshihide
Chinotaikul, Punthira
Hattori, Shingo
Clarke, Thomas A.
Shi, Liang
Hashimoto, Kazuhito
Ishii, Kazuyuki
Okamoto, Akihiro
author_facet Tokunou, Yoshihide
Chinotaikul, Punthira
Hattori, Shingo
Clarke, Thomas A.
Shi, Liang
Hashimoto, Kazuhito
Ishii, Kazuyuki
Okamoto, Akihiro
author_sort Tokunou, Yoshihide
collection PubMed
description 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.
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spelling pubmed-63012742019-01-15 Whole-cell circular dichroism difference spectroscopy reveals an in vivo-specific deca-heme conformation in bacterial surface cytochromes Tokunou, Yoshihide Chinotaikul, Punthira Hattori, Shingo Clarke, Thomas A. Shi, Liang Hashimoto, Kazuhito Ishii, Kazuyuki Okamoto, Akihiro Chem Commun (Camb) Chemistry 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. Royal Society of Chemistry 2018-12-25 2018-11-07 /pmc/articles/PMC6301274/ /pubmed/30403202 http://dx.doi.org/10.1039/c8cc06309e Text en This journal is © The Royal Society of Chemistry 2018 http://creativecommons.org/licenses/by/3.0/ This article is freely available. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence (CC BY 3.0)
spellingShingle Chemistry
Tokunou, Yoshihide
Chinotaikul, Punthira
Hattori, Shingo
Clarke, Thomas A.
Shi, Liang
Hashimoto, Kazuhito
Ishii, Kazuyuki
Okamoto, Akihiro
Whole-cell circular dichroism difference spectroscopy reveals an in vivo-specific deca-heme conformation in bacterial surface cytochromes
title Whole-cell circular dichroism difference spectroscopy reveals an in vivo-specific deca-heme conformation in bacterial surface cytochromes
title_full Whole-cell circular dichroism difference spectroscopy reveals an in vivo-specific deca-heme conformation in bacterial surface cytochromes
title_fullStr Whole-cell circular dichroism difference spectroscopy reveals an in vivo-specific deca-heme conformation in bacterial surface cytochromes
title_full_unstemmed Whole-cell circular dichroism difference spectroscopy reveals an in vivo-specific deca-heme conformation in bacterial surface cytochromes
title_short Whole-cell circular dichroism difference spectroscopy reveals an in vivo-specific deca-heme conformation in bacterial surface cytochromes
title_sort whole-cell circular dichroism difference spectroscopy reveals an in vivo-specific deca-heme conformation in bacterial surface cytochromes
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6301274/
https://www.ncbi.nlm.nih.gov/pubmed/30403202
http://dx.doi.org/10.1039/c8cc06309e
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