Mediator-free enzymatic electrosynthesis of formate by the Methanococcus maripaludis heterodisulfide reductase supercomplex Journal Article
| Authors: | Lienemann, M.; Deutzmann, J. S.; Milton, R. D.; Sahin, M.; Spormann, A. M. |
| Article Title: | Mediator-free enzymatic electrosynthesis of formate by the Methanococcus maripaludis heterodisulfide reductase supercomplex |
| Abstract: | Electrosynthesis of formate is a promising technology to convert CO2 and electricity from renewable sources into a biocompatible, soluble, non-flammable, and easily storable compound. In the model methanogen Methanococcus maripaludis, uptake of cathodic electrons was shown to proceed indirectly via formation of formate or H2 by undefined, cell-derived enzymes. Here, we identified that the multi-enzyme heterodisulfide reductase supercomplex (Hdr-SC) of M. maripaludis is capable of direct electron uptake and catalyzes rapid H2 and formate formation in electrochemical reactors (−800 mV vs Ag/AgCl) and in Fe(0) corrosion assays. In Fe(0) corrosion assays and electrochemical reactors, purified Hdr-SC primarily catalyzed CO2 reduction to formate with a coulombic efficiency of 90% in the electrochemical cells for 5 days. Thus, this report identified the first enzyme that stably catalyzes the mediator-free electrochemical reduction of CO2 to formate, which can serve as the basis of an enzyme electrode for sustained electrochemical production of formate. © 2018 |
| Keywords: | biocompatibility; catalysis; enzymes; carbon dioxide; reduction; bacteria; electrodes; direct electron transfer; electrochemical synthesis of formate; enzyme electrode; heterodisulfide reductase; microbial electrosynthesis; corrosion; electrolytic reduction; enzyme electrodes; coulombic efficiency; electrochemical reactor; electrochemical reductions; electrochemical synthesis; methanococcus maripaludis; electrochemical electrodes |
| Journal Title: | Bioresource Technology |
| Volume: | 254 |
| ISSN: | 0960-8524 |
| Publisher: | Elsevier B.V. |
| Date Published: | 2018-04-01 |
| Start Page: | 278 |
| End Page: | 283 |
| Language: | English |
| DOI: | 10.1016/j.biortech.2018.01.036 |
| PROVIDER: | scopus |
| PUBMED: | 29413934 |
| DOI/URL: | |
| Notes: | Article -- Export Date: 2 April 2018 -- Source: Scopus |
