Electrochemical Study on the Extracellular Electron Transfer Pathway from Shewanella Strain Hac319 to Electrodes
| Autor: | Kenji Kano, Yuki Kitazumi, Ryosuke Takeuchi, Osamu Shirai, Yu Sugimoto, Jun Ogawa |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Shewanella animal structures Hemeprotein Flavin Mononucleotide 030106 microbiology Flavin mononucleotide Electron donor Redox Analytical Chemistry Electron Transport 03 medical and health sciences Electron transfer chemistry.chemical_compound Electrochemistry Lactic Acid Electrodes chemistry.chemical_classification Cyanides biology Chemistry Electron acceptor biology.organism_classification Electron transport chain 030104 developmental biology Biophysics Extracellular Space |
| Zdroj: | Analytical Sciences. 34:1177-1182 |
| ISSN: | 1348-2246 0910-6340 |
| DOI: | 10.2116/analsci.18p237 |
| Popis: | Shewanella can transfer electrons to various extracellular electron acceptors. We electrochemically investigated the pathway of extracellular electron transfer from Shewanella strain Hac319 to electrodes. A resting cell suspension of Shewanella strain Hac319 containing lactate produced a steady-state sigmoidal wave in the presence of flavin mononucleotide (FMN) in cyclic voltammetry, but not in the absence of FMN. A harvested cell suspension without cell-washing also produced a similar catalytic wave without any external addition of free FMN. The midpoint potentials of the two sigmoidal waves were identical to the redox potential of free FMN. The data indicate that FMN secreted from the Shewanella strain Hac319 works as an electron-transfer mediator from the cell to electrodes. An addition of cyanide to a resting cell suspension of Shewanella strain Hac319 increased the rate of the FMN reduction in the presence of lactate, while it decreased the respiration rate. By considering the fact that cyanide is coordinated to the heme moiety of hemoproteins and shifts the redox potential to the negative potential side, the data indicate that the electron derived from lactate is predominantly transferred in a down-hill mode from an electron donor with a redox potential more negative than that of FMN without going through outer membrane cytochromes c molecules. |
| Databáze: | OpenAIRE |
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