| Literature DB >> 27193068 |
Chong-Yong Lee1, Bertrand Reuillard1, Katarzyna P Sokol1, Theodoros Laftsoglou2, Colin W J Lockwood3, Sam F Rowe3, Ee Taek Hwang2, Juan C Fontecilla-Camps4, Lars J C Jeuken2, Julea N Butt3, Erwin Reisner1.
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.Entities:
Year: 2016 PMID： 27193068 DOI： 10.1039/c6cc02721k
Source DB: PubMed Journal: Chem Commun (Camb) ISSN： 1359-7345 Impact factor: 6.222