Issue 46, 2016

A decahaem cytochrome as an electron conduit in protein–enzyme redox processes

Abstract

The decahaem cytochrome MtrC from Shewanella oneidensis MR-1 was employed as a protein electron conduit between a porous indium tin oxide electrode and redox enzymes. Using a hydrogenase and a fumarate reductase, MtrC was shown as a suitable and efficient diode to shuttle electrons to and from the electrode with the MtrC redox activity regulating the direction of the enzymatic reactions.

Graphical abstract: A decahaem cytochrome as an electron conduit in protein–enzyme redox processes

Supplementary files

Article information

Article type
Communication
Submitted
31 Mar 2016
Accepted
04 May 2016
First published
04 May 2016
This article is Open Access
Creative Commons BY license

Chem. Commun., 2016,52, 7390-7393

Author version available

A decahaem cytochrome as an electron conduit in protein–enzyme redox processes

C. Lee, B. Reuillard, K. P. Sokol, T. Laftsoglou, C. W. J. Lockwood, S. F. Rowe, E. T. Hwang, J. C. Fontecilla-Camps, L. J. C. Jeuken, J. N. Butt and E. Reisner, Chem. Commun., 2016, 52, 7390 DOI: 10.1039/C6CC02721K

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