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Issue 46, 2016
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A decahaem cytochrome as an electron conduit in protein–enzyme redox processes

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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

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Publication details

The article was received on 31 Mar 2016, accepted on 04 May 2016 and first published on 04 May 2016


Article type: Communication
DOI: 10.1039/C6CC02721K
Citation: Chem. Commun., 2016,52, 7390-7393
  • Open access: Creative Commons BY license
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    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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