期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 53, 期 41, 页码 10988-10991出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201407004
关键词
cytochromes; electron transfer; in vivo studies; microbial electrosynthesis; riboflavins
资金
- Japan Society for Promotion of Science (JSPS), KAKENHI [24000010]
- Grants-in-Aid for Scientific Research [24000010] Funding Source: KAKEN
The iron-reducing bacterium Shewanella oneidensis MR-1 has a dual directional electronic conduit involving 40 heme redox centers in flavin-binding outer-membrane c-type cytochromes (OM c-Cyts). While the mechanism for electron export from the OM c-Cyts to an anode is well understood, how the redox centers in OM c-Cyts take electrons from a cathode has not been elucidated at the molecular level. Electrochemical analysis of live cells during switching from anodic to cathodic conditions showed that altering the direction of electron flow does not require gene expression or protein synthesis, but simply redox potential shift about 300 mV for a flavin cofactor interacting with the OM c-Cyts. That is, the redox bifurcation of the riboflavin cofactor in OM c-Cyts switches the direction of electron conduction in the biological conduit at the cell-electrode interface to drive bacterial metabolism as either anode or cathode catalysts.
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