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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Main Authors: 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
Outros Autores: Law Enforcement
Idioma:inglês
Publicado em: Royal Society of Chemistry 2019
Acesso em linha:https://demo7.dspace.org/handle/123456789/463
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author 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
author2 Law Enforcement
author_browse Butt, Julea N
Fontecilla-Camps, Juan C
Hwang, Ee Taek
Jeuken, Lars JC
Laftsoglou, Theodoros
Law Enforcement
Lee, Chong-Yong
Lockwood, Colin WJ
Reisner, Erwin
Reuillard, Bertrand
Rowe, Sam F
Sokol, Katarzyna
author_facet Law Enforcement
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
author_sort Lee, Chong-Yong
collection DSpace
description 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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institution DSPACE.FCHPT
language English
publishDate 2019
publishDateRange 2019
publishDateSort 2019
publisher Royal Society of Chemistry
publisherStr Royal Society of Chemistry
record_format dspace
spelling oai:localhost:123456789-4632021-04-07T16:30:12Z A decahaem cytochrome as an electron conduit in protein-enzyme redox processes 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 Law Enforcement Law and Development 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. 2019-04-26T08:57:16Z 2019-04-26T08:57:16Z 04/05/16 https://demo7.dspace.org/handle/123456789/463 en Royal Society of Chemistry
spellingShingle 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
A decahaem cytochrome as an electron conduit in protein-enzyme redox processes
title A decahaem cytochrome as an electron conduit in protein-enzyme redox processes
title_full A decahaem cytochrome as an electron conduit in protein-enzyme redox processes
title_fullStr A decahaem cytochrome as an electron conduit in protein-enzyme redox processes
title_full_unstemmed A decahaem cytochrome as an electron conduit in protein-enzyme redox processes
title_short A decahaem cytochrome as an electron conduit in protein-enzyme redox processes
title_sort decahaem cytochrome as an electron conduit in protein enzyme redox processes
url https://demo7.dspace.org/handle/123456789/463
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