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dc.contributor.authorAuthorOsorio, Manuel I.
dc.contributor.authorAuthorBruna, Nicolás
dc.contributor.authorAuthorGarcía, Víctor
dc.contributor.authorAuthorGonzález-Rodríguez, Lisdelys
dc.contributor.authorAuthorLeal, Matías S.
dc.contributor.authorAuthorSalgado, Francisco
dc.contributor.authorAuthorVargas-Reyes, Matías
dc.contributor.authorAuthorGonzález-Nilo, Fernando
dc.contributor.authorAuthorPérez-Donoso, José M.
dc.contributor.authorAuthorYáñez, Osvaldo
dc.date.accessionedDate Accessioned2024-09-03T19:17:46Z
dc.date.availableDate Available2024-09-03T19:17:46Z
dc.date.issuedDate Issued2023
dc.identifier.citationReferencia BibliográficaInternational Journal of Molecular Sciences, 24(1), 15 p.
dc.identifier.issnISSN1661-6596
dc.identifier.uriURIhttp://repositorio.udla.cl/xmlui/handle/udla/1359
dc.identifier.uriURIhttps://www.mdpi.com/journal/ijms
dc.description.abstractAbstractXenobiotic reductase B (XenB) catalyzes the reduction of the aromatic ring or nitro groups of nitroaromatic compounds with methyl, amino or hydroxyl radicals. This reaction is of biotechnological interest for bioremediation, the reuse of industrial waste or the activation of prodrugs. However, the structural factors that explain the binding of XenB to different substrates are unknown. Molecular dynamics simulations and quantum mechanical calculations were performed to identify the residues involved in the formation and stabilization of the enzyme/substrate complex and to explain the use of different substrates by this enzyme. Our results show that Tyr65 and Tyr335 residues stabilize the ligands through hydrophobic interactions mediated by the aromatic rings of these aminoacids. The higher XenB activity determined with the substrates 1,3,5-trinitrobenzene and 2,4,6-trinitrotoluene is consistent with the lower energy of the highest occupied molecular orbital (LUMO) orbitals and a lower energy of the homo orbital (LUMO), which favors electrophile and nucleophilic activity, respectively. The electrostatic potential maps of these compounds suggest that the bonding requires a large hydrophobic region in the aromatic ring, which is promoted by substituents in ortho and para positions. These results are consistent with experimental data and could be used to propose point mutations that allow this enzyme to process new molecules of biotechnological interest.
dc.format.extentdc.format.extent15 páginas
dc.format.extentdc.format.extent4.330Mb
dc.format.mimetypedc.format.mimetypePDF
dc.language.isoLanguage ISOeng
dc.publisherPublisherMDPI
dc.rightsRightsCreative Commons Attribution (CC BY)
dc.sourceSourcesInternational Journal of Molecular Sciences
dc.subjectSubjectMolecular dynamics simulation
dc.subjectSubjectSubstrate promiscuity of enzymes
dc.subjectSubjectNitroaromatic compound reactivity
dc.subjectSubjectProtein – ligand interactions
dc.subject.lcshdc.subject.lcshTeoría cuántica
dc.titleTitleStructural factors that determine the activity of the xenobiotic reductase B enzyme from pseudomonas putida on nitroaromatic compounds
dc.typeDocument TypeArtículo
dc.udla.catalogadordc.udla.catalogadorCBM
dc.udla.indexdc.udla.indexScience Citation Index Expanded
dc.udla.indexdc.udla.indexScopus
dc.udla.indexdc.udla.indexAcademic Search Ultimate
dc.udla.indexdc.udla.indexDOAJ
dc.udla.indexdc.udla.indexBiomedical Reference Collection: Corporate Edition
dc.udla.indexdc.udla.indexEMBASE
dc.udla.indexdc.udla.indexMEDLINE
dc.identifier.doidc.identifier.doi10.3390/ijms24010400
dc.facultaddc.facultadFacultad de Ingeniería y Negocios


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