A decahaem cytochrome as an electron conduit in protein-enzyme redox processes.
A decahaem cytochrome as an electron conduit in protein-enzyme redox processes.
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DOI:
10.1039/c6cc02721k
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发表时间:
2016-05
影响因子:
4.9
通讯作者:
Chong‐Yong Lee;Bertrand Reuillard;Katarzyna P. Sokol;T. Laftsoglou;Colin W. J. Lockwood;Sam F. Rowe;E. Hwang;J. Fontecilla-Camps;L. Jeuken;J. Butt;E. Reisner
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文献类型:
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作者:
Chong‐Yong Lee;Bertrand Reuillard;Katarzyna P. Sokol;T. Laftsoglou;Colin W. J. Lockwood;Sam F. Rowe;E. Hwang;J. Fontecilla-Camps;L. Jeuken;J. Butt;E. Reisner
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.