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The amino acids motif-32GSSYN36-in the catalytic domain of E. coli flavorubredoxin NO reductase is essential for its activity

2021-08Artigo científico Acesso aberto
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dc.contributor.authorMartins, Maria C.
dc.contributor.authorFernandes, Susana F.
dc.contributor.authorSalgueiro, Bruno A.
dc.contributor.authorSoares, Jéssica C.
dc.contributor.authorRomão, Célia V.
dc.contributor.authorSoares, Cláudio M.
dc.contributor.authorLousa, Diana
dc.contributor.authorFolgosa, Filipe
dc.contributor.authorTeixeira, Miguel
dc.contributor.institutionInstituto de Tecnologia Química e Biológica António Xavier (ITQB)
dc.contributor.pblMDPI - Multidisciplinary Digital Publishing Institute
dc.date.accessioned2021-12-06T23:42:22Z
dc.date.available2021-12-06T23:42:22Z
dc.date.issued2021-08
dc.descriptionFunding Information: Funding: This study was financially supported by the Portuguese Fundação para a Ciência e Tec-nologia (FCT), grants PTDC/BIA-BQM/27959/2017 and PTDC/BIA-BQM/0562/2020, and Project MOSTMICRO-ITQB with references UIDB/04612/2020 and UIDP/04612/2020. This project has also received funding from the European Union’s Horizon 2020 research and innovation program under grant agreement 810856. MCM is the recipient of FCT grant SFRH/BD/143651/2019. BAS is the recipient of FCT grant DFA/BD/8066/2020. Funding Information: This study was financially supported by the Portuguese Funda??o para a Ci?ncia e Tecnologia (FCT), grants PTDC/BIA-BQM/27959/2017 and PTDC/BIA-BQM/0562/2020, and Project MOSTMICRO-ITQB with references UIDB/04612/2020 and UIDP/04612/2020. This project has also received funding from the European Union?s Horizon 2020 research and innovation program under grant agreement 810856. MCM is the recipient of FCT grant SFRH/BD/143651/2019. BAS is the recipient of FCT grant DFA/BD/8066/2020. Publisher Copyright: © 2021 by the authors. Licensee MDPI, Basel, Switzerland.
dc.description.abstractFlavodiiron proteins (FDPs) are a family of modular and soluble enzymes endowed with nitric oxide and/or oxygen reductase activities, producing N2O or H2O, respectively. The FDP from Escherichia coli, which, apart from the two core domains, possesses a rubredoxin-like domain at the C-terminus (therefore named flavorubredoxin (FlRd)), is a bona fide NO reductase, exhibiting O2 reducing activity that is approximately ten times lower than that for NO. Among the flavorubredoxins, there is a strictly conserved amino acids motif,-G[S,T]SYN-, close to the catalytic diiron center. To assess its role in FlRd’s activity, we designed several site-directed mutants, replacing the conserved residues with hydrophobic or anionic ones. The mutants, which maintained the general characteristics of the wild type enzyme, including cofactor content and integrity of the diiron center, revealed a decrease of their oxygen reductase activity, while the NO reductase activity—specifically, its physiological function—was almost completely abolished in some of the mutants. Molecular modeling of the mutant proteins pointed to subtle changes in the predicted structures that resulted in the reduction of the hydration of the regions around the conserved residues, as well as in the elimination of hydrogen bonds, which may affect proton transfer and/or product release.en
dc.description.versionpublished
dc.format.extent3342918
dc.identifier.doi10.3390/catal11080926
dc.identifier.issn2073-4344
dc.identifier.otherPURE: 33146388
dc.identifier.otherPURE UUID: 572948c6-9e64-4c20-aa88-2df71f28e03d
dc.identifier.otherScopus: 85111418541
dc.identifier.otherORCID: /0000-0003-1154-556X/work/104340367
dc.identifier.urihttp://hdl.handle.net/10362/128786
dc.identifier.urlhttps://www.scopus.com/pages/publications/85111418541
dc.language.isoeng
dc.peerreviewedyes
dc.subjectDiiron
dc.subjectFlavodiiron proteins
dc.subjectFlavorubredoxin
dc.subjectNitric oxide reductase
dc.subjectNitrosative stress
dc.subjectOxygen reductase
dc.subjectCatalysis
dc.subjectPhysical and Theoretical Chemistry
dc.titleThe amino acids motif-32GSSYN36-in the catalytic domain of E. coli flavorubredoxin NO reductase is essential for its activityen
dc.typejournal article
degois.publication.issue8
degois.publication.titleCatalysts
degois.publication.volume11
dspace.entity.typePublication
rcaap.rightsopenAccess

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