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.
Original language | English |
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Pages (from-to) | 7390-7390 |
Number of pages | 4 |
Journal | Chemical Communications |
Volume | 52 |
Issue number | 46 |
Early online date | 4 May 2016 |
DOIs | |
Publication status | Published - 11 Jun 2016 |