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

Authors

Chong Yong Lee, University of WollongongFollow
Bertrand Reuillard, University of Cambridge
Katarzyna Sokol, University of Cambridge
Theodoros Laftsoglou, University of Leeds
Colin Lockwood, University of East Anglia
Sam Rowe, University of East Anglia
Ee Taek Hwang, University of Leeds
Juan Fontecilla-Camps, Universite Grenoble Alpes
Lars J. C Jeuken, University of Leeds
Julea N. Butt, University of East Anglia
Erwin Reisner, University of Cambridge

RIS ID

111948

Publication Details

Lee, C., Reuillard, B., Sokol, K. P., Laftsoglou, T., Lockwood, C. W. J., Rowe, S. F., Hwang, E., Fontecilla-Camps, J. C., Jeuken, L. J. C., Butt, J. N. & Reisner, E. (2016). A decahaem cytochrome as an electron conduit in protein-enzyme redox processes. Chemical Communications, 52 (46), 7390-7393.

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.