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Electroenzymatic CO2 Reduction Using Formate Dehydrogenase

2025-06-12Artigo científico Acesso aberto
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dc.contributor.authorPaul, Navendu
dc.contributor.authorMoura, Isabel
dc.contributor.authorMaia, Luísa B.
dc.contributor.authorCordas, Cristina M.
dc.contributor.authorMoura, Jose J.G.
dc.contributor.institutionLAQV@REQUIMTE
dc.contributor.pblWILEY-V C H VERLAG GMBH
dc.date.accessioned2025-08-20T21:21:00Z
dc.date.available2025-08-20T21:21:00Z
dc.date.issued2025-06-12
dc.descriptionFunding Information: This work was supported by the PTDC/BTA-BTA/0935/2020 project and by the Associate Laboratory for Green Chemistry-LAQV (UID/50006/2023), which are financed by national funds from Fundação para a Ciência e a Tecnologia, MCTES (FCT/MCTES). Publisher Copyright: © 2025 The Author(s). ChemElectroChem published by Wiley-VCH GmbH.
dc.description.abstractThe electrocatalytic reduction of carbon dioxide (CO2) to formate by the enzyme formate dehydrogenase (FDH) makes use of the enzyme's observed reversibility, offering a promising strategy for the mitigation of CO2 and the production of value-added compounds. To enhance the catalytic potential of Desulfovibrio desulfuricans FDH (DdFDH), a range of artificial and natural redox cofactors is investigated using electrochemical methods. These studies included direct (nonmediated) conditions and mediated conditions employing viologens (methyl and benzyl viologens), and small heme proteins (cytochromes). Methyl viologen acts as an efficient mediator for CO2 reduction, achieving a very high current density of 216 μA cm−2. The studies of the different small proteins, namely cytochrome split-soret (cyt SS), cytochrome c3 (cyt c3), and cytochrome c552 (cyt c552), allow the identification of the potential natural physiological partners. These isolated cytochromes, from the same organism, are electrochemically characterized, from which detailed redox processes are determined and later used as mediators to explore DdFDH catalytic activity in both formate oxidation and CO2 reduction. Best results are attained with cytochrome cyt SS and cyt c3, increasing the electrocatalytic activity for formate oxidation by 7.5 times and 5.8 times, respectively.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent7
dc.format.extent1327021
dc.identifier.doi10.1002/celc.202500100
dc.identifier.issn2196-0216
dc.identifier.otherPURE: 119134852
dc.identifier.otherPURE UUID: 1a8be04d-3f8b-4a60-b232-0acff6172bde
dc.identifier.otherScopus: 105007912247
dc.identifier.otherWOS: 001509024500001
dc.identifier.otherORCID: /0000-0002-7892-8955/work/190210893
dc.identifier.otherORCID: /0000-0002-6901-6591/work/190211619
dc.identifier.otherORCID: /0000-0002-4726-2388/work/190212225
dc.identifier.urihttp://hdl.handle.net/10362/186685
dc.identifier.urlhttps://www.scopus.com/pages/publications/105007912247
dc.identifier.urlhttps://www.webofscience.com/wos/woscc/full-record/WOS:001509024500001
dc.language.isoeng
dc.peerreviewedyes
dc.relationinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBTA-BTA%2F0935%2F2020/PT
dc.subjectBioelectrochemistry
dc.subjectCO2 reductions
dc.subjectCytochromes
dc.subjectEnzymatic activities
dc.subjectFormate dehydrogenases
dc.subjectCatalysis
dc.subjectElectrochemistry
dc.titleElectroenzymatic CO2 Reduction Using Formate Dehydrogenaseen
dc.title.subtitleDirect and Mediated Catalysisen
dc.typejournal article
degois.publication.firstPage1
degois.publication.issue5
degois.publication.lastPage7
degois.publication.titleChemelectrochem
degois.publication.volume12
dspace.entity.typePublication
oaire.awardNumberPTDC/BTA-BTA/0935/2020
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBTA-BTA%2F0935%2F2020/PT
oaire.fundingStream3599-PPCDT
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccess
relation.isProjectOfPublicationc0112d94-7b16-4393-864c-c09331039eed
relation.isProjectOfPublication.latestForDiscoveryc0112d94-7b16-4393-864c-c09331039eed

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