%0 Journal Article
%A Terán More, Aaron
%A Jaafar, Aida
%A Sánchez Peláez, Ana Edilia
%A Torralba Martínez, María Del Carmen
%A Gutiérrez Alonso, Ángel
%T Design and catalytic studies of structural and functional models of the catechol oxidase enzyme.
%D 2020
%U https://hdl.handle.net/20.500.14352/115771
%X The catechol oxidase activity of three copper/bicompartmental salen derivatives has been studied. One mononuclear, [CuL](1), one homometallic, [Cu2L(NO3)2] (2), and one heterometallic, [CuMnL(NO3)2] (3) complexes were obtained using the ligand H2L= N,N′-bis(3-methoxysalicylidene)-1,3-propanediamine through different synthetic methods (electrochemical, chemical and solid state reaction). The structural data indicate that the metal ion disposition models the active site of type-3 copper enzymes, such as catechol oxidase. In this way, their ability to act as functional models of the enzyme has been spectrophotometrically determined by monitorization of the oxidation of 3,5-di-tert-butylcatechol (3,5-DTBC) to 3,5-ditert-butyl-o-benzoquinone (3,5-DTBQ). All the complexes show significant catalytic activity with ratio constants (kobs) lying in the range (223–294) × 10–4 min−1. A thorough kinetic study was carried out for complexes 2 and 3, since they show structural similarities with the catechol oxidase enzyme. The greatest catalytic activity was found for the homonuclear dicopper compound (2) with a turnover value (kcat) of (3.89 ± 0.05) × 106 h−1, which it is the higher reported to date, comparable to the enzyme itself (8.25 × 106 h−1).
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