Modelos miméticos de catecol dioxigenase e catecol oxidase: correlação entre estrutura e atividade catalítica de complexos mononucleares de ferro(III) e binucleares de cobre(II) contendo bases de Schiff

• Ano de defesa: 2014
• Autor(a) principal: Cruz Júnior, José Wilmo da
• Orientador(a): Dockal, Edward Ralph
• Tipo de documento: Tese
• Tipo de acesso: Acesso aberto
• Idioma: por
• Instituição de defesa: Universidade Federal de São Carlos
• Programa de Pós-Graduação: Programa de Pós-Graduação em Química - PPGQ
• País: BR
• Palavras-chave em Português: Química inorgânica; Schiff, Bases de; Oxidação de catecóis; Modelos miméticos
• Área do conhecimento CNPq: CIENCIAS EXATAS E DA TERRA::QUIMICA
• Link de acesso: https://repositorio.ufscar.br/handle/ufscar/6342

In this work binuclear copper(II) complexes and mononuclear iron(III) complexes were studied as functional mimetic models of enzymes capable of catalyze the oxidation of catechols. Different structures of the complexes were obtained by synthesizing them with different Schiff bases, which possesses imine groups with aliphatic chains containing groups ranging from two to six carbon atoms between the nitrogen atoms, as well as cyclic substituted aromatic species between these atoms. These structures have allowed structural and electronic effects to be evaluated and correlated with the catalytic activity of their complexes. The binuclear copper complexes showed excellent catalytic efficiency in transforming the substrate 3,5-di-tert-butylcatechol to its respective quinone. The kinetic parameters obtained allowed the evaluation of how and which structural effects affect their catalytic efficiencies, being observed an increase in affinity between catalyst and substrate with increasing carbon chain between imines. It was also observed that the presence of substituents in compounds with aromatic diimines causes a lesser affinity between catalyzer and substrate and consequently a low catalytic efficiency. Catalytic assays with the iron(III) complexes have shown that regardless of the structural changes caused, none of them presented activity similar to the enzyme catechol dioxygenase. But those complexes which catalyzed the oxidation of the substrate to its respective quinone, being these changes accompanied for 24 hours of reaction. Although the substrate conversions were slow and low, trends were observed from correlations between structure and catalytic activity. The percentages of 3,5-di-tert-butilquinone obtained for the best catalysts among these complexes suggests that there is a step of forming a catalytically active species during the reaction time.