Publication:
Biocatalytic oxidation of phenolic compounds by bovine methemoglobin in the presence of H2O2: quantitative structure-activity relationships

dc.affiliation.dptoUC3M. Departamento de Ciencia e Ingeniería de Materiales e Ingeniería Químicaes
dc.affiliation.grupoinvUC3M. Grupo de Investigación: Síntesis y Procesado de Materialeses
dc.contributor.authorPérez Prior, María Teresa
dc.contributor.authorGomez-Bombarelli, Rafael
dc.contributor.authorGonzález-Sánchez, M.I.
dc.contributor.authorValero, E.
dc.date.accessioned2021-02-08T13:32:38Z
dc.date.available2021-02-08T13:32:38Z
dc.date.issued2012-11-30
dc.description.abstractIn the present work, 13 p-substituted phenols with different functional groups have been systematically evaluated as metHb substrates by means of HPLC analysis. Non-hyperbolic kinetics were observed and Hill coefficients in the 0.37&-1.00 range were obtained. The catalytic constants and the Hill coefficients were found to be quantitatively correlated with two independent variables: the energy level of the highest-occupied molecular orbital (EHOMO), which describes the intrinsic redox activity of the substrates and the pKa-values, which are related to substrate ionization. Oxygen evolution in the presence of each phenol derivative was also measured, and good correlation between peroxidase-like and catalase-like activities of the protein was observed. It is also shown that bovine metHb, although less active than other peroxidases, may represent a good alternative from an economical point of view for phenol removal processes. The equations here obtained may serve as a basis to further explore the potential use of metHb-mediated reactions in the treatment of phenols in wastewaters and to predict which phenol will be removed most efficiently under this treatment with satisfactory reliability.en
dc.description.sponsorshipThis work has been supported by the Project POII10-0235-8597 from the Regional Ministry of Education and Science of Castilla-La Mancha (JCCM, Spain). M.T.P.P. also thanks this organisation for a postdoctoral grant.en
dc.format.extent9es
dc.identifier.bibliographicCitationJournal of hazardous materials, Vol. 241-242, Nov. 2012, Pp. 207-215en
dc.identifier.doihttps://doi.org/10.1016/j.jhazmat.2012.09.028
dc.identifier.issn0304-3894
dc.identifier.issn1873-3336 (online)
dc.identifier.publicationfirstpage207es
dc.identifier.publicationlastpage215es
dc.identifier.publicationtitleJOURNAL OF HAZARDOUS MATERIALSen
dc.identifier.publicationvolume241-242es
dc.identifier.urihttps://hdl.handle.net/10016/31880
dc.identifier.uxxiAR/0000026979
dc.language.isoenges
dc.publisherElsevier B.V.en
dc.rights© 2012 Elsevier B.V. All rights reserved.en
dc.rightsAtribución-NoComercial-SinDerivadas 3.0 España*
dc.rights.accessRightsopen accessen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/es/*
dc.subject.ecienciaMaterialeses
dc.subject.otherHemoglobinen
dc.subject.otherQSARen
dc.subject.otherPhenolic compoundsen
dc.subject.otherPeroxidase-like activityen
dc.subject.otherCatalase-like activityen
dc.titleBiocatalytic oxidation of phenolic compounds by bovine methemoglobin in the presence of H2O2: quantitative structure-activity relationshipsen
dc.typeresearch article*
dc.type.hasVersionAM*
dspace.entity.typePublication
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