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Article Dans Une Revue Chemical Communications Année : 2016

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

Résumé

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.

Dates et versions

hal-01338650 , version 1 (29-06-2016)

Identifiants

Citer

Chong-Yong Lee, Bertrand Reuillard, Katarzyna P Sokol, Theodoros Laftsoglou, Colin W J Lockwood, et al.. A decahaem cytochrome as an electron conduit in protein-enzyme redox processes.. Chemical Communications, 2016, 52 (46), pp.7390-3. ⟨10.1039/c6cc02721k⟩. ⟨hal-01338650⟩
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