Mediator-free enzymatic electrosynthesis of formate by the Methanococcus maripaludis heterodisulfide reductase supercomplex

Michael Lienemann, Jörg Stefan Deutzmann, Ross Dean Milton, Merve Sahin, Alfred Michael Spormann

Research output: Contribution to journal › Article › Scientific › peer-review

16 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)278-283
Number of pages6
JournalBioresource Technology
Volume254
Early online date9 Jan 2018
DOIs
Publication statusPublished - 1 Apr 2018
MoE publication typeA1 Journal article-refereed

Fingerprint

formic acid
Enzymes
enzyme
Assays
Enzyme electrodes
Corrosion
Methanogens
corrosion
Electrochemical cells
Electrons
assay
electron
Electricity
electricity
electrode
heterodisulfide reductase
Oxidoreductases

Keywords

  • Direct electron transfer
  • Electrochemical synthesis of formate
  • Enzyme electrode
  • Heterodisulfide reductase
  • Microbial electrosynthesis

Cite this

Lienemann, Michael ; Deutzmann, Jörg Stefan ; Milton, Ross Dean ; Sahin, Merve ; Spormann, Alfred Michael. / Mediator-free enzymatic electrosynthesis of formate by the Methanococcus maripaludis heterodisulfide reductase supercomplex. In: Bioresource Technology. 2018 ; Vol. 254. pp. 278-283.
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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.",
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Lienemann, M, Deutzmann, JS, Milton, RD, Sahin, M & Spormann, AM 2018, 'Mediator-free enzymatic electrosynthesis of formate by the Methanococcus maripaludis heterodisulfide reductase supercomplex', Bioresource Technology, vol. 254, pp. 278-283. https://doi.org/10.1016/j.biortech.2018.01.036

Mediator-free enzymatic electrosynthesis of formate by the Methanococcus maripaludis heterodisulfide reductase supercomplex. / Lienemann, Michael; Deutzmann, Jörg Stefan; Milton, Ross Dean; Sahin, Merve; Spormann, Alfred Michael.

In: Bioresource Technology, Vol. 254, 01.04.2018, p. 278-283.

Research output: Contribution to journal › Article › Scientific › peer-review

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T1 - Mediator-free enzymatic electrosynthesis of formate by the Methanococcus maripaludis heterodisulfide reductase supercomplex

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AU - Deutzmann, Jörg Stefan

AU - Milton, Ross Dean

AU - Sahin, Merve

AU - Spormann, Alfred Michael

PY - 2018/4/1

Y1 - 2018/4/1

N2 - 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.

AB - 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.

KW - Direct electron transfer

KW - Electrochemical synthesis of formate

KW - Enzyme electrode

KW - Heterodisulfide reductase

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Lienemann M, Deutzmann JS, Milton RD, Sahin M, Spormann AM. Mediator-free enzymatic electrosynthesis of formate by the Methanococcus maripaludis heterodisulfide reductase supercomplex. Bioresource Technology. 2018 Apr 1;254:278-283. https://doi.org/10.1016/j.biortech.2018.01.036

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