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Toward the Mechanistic Understanding of Enzymatic CO2 Reduction

2020-03-20Artigo científico Acesso aberto
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dc.contributor.authorOliveira, Ana Rita
dc.contributor.authorMota, Cristiano
dc.contributor.authorMourato, Cláudia
dc.contributor.authorDomingos, Renato M.
dc.contributor.authorSantos, Marino F. A.
dc.contributor.authorGesto, Diana
dc.contributor.authorGuigliarelli, Bruno
dc.contributor.authorSantos-Silva, Teresa
dc.contributor.authorRomão, Maria João
dc.contributor.authorCardoso Pereira, Inês A.
dc.contributor.institutionInstituto de Tecnologia Química e Biológica António Xavier (ITQB)
dc.contributor.institutionUCIBIO - Applied Molecular Biosciences Unit
dc.contributor.institutionDQ - Departamento de Química
dc.contributor.institutionDCV - Departamento de Ciências da Vida
dc.contributor.pblACS - American Chemical Society
dc.date.accessioned2021-02-19T23:01:44Z
dc.date.available2021-02-19T23:01:44Z
dc.date.issued2020-03-20
dc.descriptionSFRH/BD/116515/2014 PTDC/BBB-EBB/2723/2014 UID/Multi/04378/2019 grant agreement number 810856
dc.description.abstractReducing CO2 is a challenging chemical transformation that biology solves easily, with high efficiency and specificity. In particular, formate dehydrogenases are of great interest since they reduce CO2 to formate, a valuable chemical fuel and hydrogen storage compound. The metal-dependent formate dehydrogenases of prokaryotes can show high activity for CO2 reduction. Here, we report an expression system to produce recombinant W/Sec-FdhAB from Desulfovibrio vulgaris Hildenborough fully loaded with cofactors, its catalytic characterization and crystal structures in oxidized and reduced states. The enzyme has very high activity for CO2 reduction and displays remarkable oxygen stability. The crystal structure of the formate-reduced enzyme shows Sec still coordinating the tungsten, supporting a mechanism of stable metal coordination during catalysis. Comparison of the oxidized and reduced structures shows significant changes close to the active site. The DvFdhAB is an excellent model for studying catalytic CO2 reduction and probing the mechanism of this conversion.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent13
dc.format.extent6729357
dc.identifier.doi10.1021/acscatal.0c00086
dc.identifier.issn2155-5435
dc.identifier.otherPURE: 28172778
dc.identifier.otherPURE UUID: c63ada23-a073-466e-b0b9-258f23d4220c
dc.identifier.otherScopus: 85082073064
dc.identifier.otherWOS: 000526394500038
dc.identifier.otherORCID: /0000-0002-3004-0543/work/89085925
dc.identifier.otherORCID: /0000-0002-3583-8407/work/89319986
dc.identifier.otherORCID: /0000-0002-8999-0420/work/89320955
dc.identifier.urihttp://hdl.handle.net/10362/112070
dc.identifier.urlhttps://www.scopus.com/pages/publications/85082073064
dc.language.isoeng
dc.peerreviewedyes
dc.relationinfo:eu-repo/grantAgreement/FCT/5876/147270/PT
dc.subjectCO reduction
dc.subjectformate dehydrogenase
dc.subjectmoco
dc.subjectmolybdopterin
dc.subjectoxygen-tolerance
dc.subjecttungsten
dc.subjectX-ray structure
dc.subjectCatalysis
dc.subjectGeneral Chemistry
dc.titleToward the Mechanistic Understanding of Enzymatic CO2 Reductionen
dc.typejournal article
degois.publication.firstPage3844
degois.publication.issue6
degois.publication.lastPage3856
degois.publication.titleACS Catalysis
degois.publication.volume10
dspace.entity.typePublication
oaire.awardNumberUID/Multi/04551/2013
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/5876/UID%2FMulti%2F04551%2F2013/PT
oaire.fundingStream5876
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccess
relation.isProjectOfPublication6badac1a-ccbc-4af7-bf8e-5eb9f5aeff50
relation.isProjectOfPublication.latestForDiscovery6badac1a-ccbc-4af7-bf8e-5eb9f5aeff50

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