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Int. J. Mol. Sci. 2017, 18(12), 2553; doi:10.3390/ijms18122553

Bioinspired versus Enzymatic Oxidation of Some Homologous Thionine Dyes in the Presence of Immobilized Metalloporphyrin Catalysts and Ligninolytic Enzymes

Department of Biomedical Sciences, Biochemistry Unit, University of Cagliari, 09042 Monserrato (CA), Italy
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Received: 29 October 2017 / Revised: 22 November 2017 / Accepted: 23 November 2017 / Published: 28 November 2017
(This article belongs to the Section Biochemistry, Molecular and Cellular Biology)
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Abstract

Thionines are recalcitrant and polluting textile dyes presenting various degrees of N-methylation. In this paper, a complete series of homologous thionines was used as the substrates for oxidation in the presence of a bioinspired commercial iron-porphyrin immobilized on to imidazole- and pyridine-functionalized fumed silica, to emulate the active site of ligninolytic peroxidases. The obtained catalytic adducts showed a remarkable ability to catalyze thionine dye oxidation in the presence of different oxidants such as potassium monopersulfate and hydrogen peroxide. Different oxidation patterns were obtained and mechanistically discussed, in comparison with those observed in the presence of some ligninolytic oxidizing enzymes. View Full-Text
Keywords: thionine; biomimetic; metalloporphyrins; metalloporphines; peroxidase; peroxygenase; monopersulfate; hydrogen peroxide thionine; biomimetic; metalloporphyrins; metalloporphines; peroxidase; peroxygenase; monopersulfate; hydrogen peroxide
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Cocco, G.; Cocco, A.; Sollai, F.; Sanjust, E.; Zucca, P. Bioinspired versus Enzymatic Oxidation of Some Homologous Thionine Dyes in the Presence of Immobilized Metalloporphyrin Catalysts and Ligninolytic Enzymes. Int. J. Mol. Sci. 2017, 18, 2553.

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