Síntese e caracterização de complexos de Cu(II) bioinspirados no sítio ativo de oxigenases

Abstract

Inorganic chemistry is the science that studies the behavior, properties and structures of inorganic compounds, showing numerous applications and ramifications. Bioinorganic aims, in general, to study the role and behavior of metals in biological systems. One of the biological systems of greatest interest, both pharmacologically and industrially, are enzymes. Enzymes act as biological catalysts in living organisms, possessing extraordinary catalytic efficiency and extremely high specificity, making the reaction rate in systems much higher compared to synthetic catalysts. The classes of enzymes that catalyze redox reactions in the presence of molecular oxygen are called oxygenases. Galactose oxidase is an enzyme that catalyzes the oxidation of primary alcohols to aldehydes, which can oxidize other substrates due to the presence of free radicals in its active site. Another example of an oxygenase is copper-zinc superoxide dismutase, which catalyzes the disproportionation of the superoxide radical into oxygen and hydrogen peroxide. Both have in their active site Cu(II) ions, an essential metal for various cell functions, being widely studied and used, with well-defined physical and chemical properties. Through this knowledge, it is possible to mimic enzymes by modeling new complexes with similar structures found in the active site of these enzymes. In order to study its redox properties, the objective of this work is the synthesis and characterization of two mononuclear complexes of Cu(II) with the ligand N,N’-bis(pyridinylmethylene)hydrazine. The ligand will be synthesized using methodologies adapted from the literature and characterized by spectroscopic techniques such as 1H, 13C-NMR and FT-IR. The complexes will be synthesized and also characterized by FT-IR and UV-Vis spectroscopy. As a final objective, the complexes will be tested in oxidation reactions of organic molecules such as catechols and aminophenols.