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

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 e...

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Hlavní autori: Lee, Chong-Yong, Reuillard, Bertrand, Sokol, Katarzyna, Laftsoglou, Theodoros, Lockwood, Colin WJ, Rowe, Sam F, Hwang, Ee Taek, Fontecilla-Camps, Juan C, Jeuken, Lars JC, Butt, Julea N, Reisner, Erwin
Ďalší autori: Law Enforcement
Jazyk:English
Vydavateľské údaje: Royal Society of Chemistry 2019
On-line prístup:https://demo7.dspace.org/handle/123456789/463
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Shrnutí: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.

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