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

A new interesting article has been published in Chem Commun (Camb). 2018 Nov 7. doi: 10.1039/c8cc06309e. [Epub ahead of print] and titled:

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

Authors of this article are:

Tokunou Y, Chinotaikul P, Hattori S, Clarke TA, Shi L, Hashimoto K, Ishii K, Okamoto A.

A summary of the article is shown below:

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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