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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Detalles Bibliográficos
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:
Chemistry
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
Descripción
Sumario: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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