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

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Show simple item record Pérez Prior, María Teresa Gomez-Bombarelli, Rafael González-Sánchez, M.I. Valero, E. 2021-02-08T13:32:38Z 2021-02-08T13:32:38Z 2012-11-30
dc.identifier.bibliographicCitation Journal of hazardous materials, Vol. 241-242, Nov. 2012, Pp. 207-215
dc.identifier.issn 0304-3894
dc.identifier.issn 1873-3336 (online)
dc.description.abstract In 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.
dc.description.sponsorship This 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.
dc.format.extent 9
dc.language.iso eng
dc.publisher Elsevier B.V.
dc.rights © 2012 Elsevier B.V. All rights reserved.
dc.rights Atribución-NoComercial-SinDerivadas 3.0 España
dc.subject.other Hemoglobin
dc.subject.other QSAR
dc.subject.other Phenolic compounds
dc.subject.other Peroxidase-like activity
dc.subject.other Catalase-like activity
dc.title Biocatalytic oxidation of phenolic compounds by bovine methemoglobin in the presence of H2O2: quantitative structure-activity relationships
dc.type article
dc.subject.eciencia Materiales
dc.rights.accessRights openAccess
dc.type.version acceptedVersion
dc.identifier.publicationfirstpage 207
dc.identifier.publicationlastpage 215
dc.identifier.publicationtitle JOURNAL OF HAZARDOUS MATERIALS
dc.identifier.publicationvolume 241-242
dc.identifier.uxxi AR/0000026979
dc.affiliation.dpto UC3M. Departamento de Ciencia e Ingeniería de Materiales e Ingeniería Química
dc.affiliation.grupoinv UC3M. Grupo de Investigación: Síntesis y Procesado de Materiales
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