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Terán More, Aaron Jaafar, Aida Sánchez-Peláez, Ana Edilia Torralba, Maria del Carmen Gutiérrez, Ángel 2023-10-30T12:24:40Z 2023-10-30T12:24:40Z 2020 Terán A, Jaafar A, Sánchez-Peláez AE, Torralba MC, Gutiérrez Á. Design and catalytic studies of structural and functional models of the catechol oxidase enzyme. J Biol Inorg Chem. 2020 Jun;25(4):671-683. doi: 10.1007/s00775-020-01791-2. Epub 2020 May 4. PMID: 32367388. 10.1007/s00775-020-01791-2 https://hdl.handle.net/20.500.14352/88491 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-di-tert-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). eng http://creativecommons.org/licenses/by-nc-nd/4.0/ open access Attribution-NonCommercial-NoDerivatives 4.0 International Design and catalytic studies of structural and functional models of the catechol oxidase enzyme journal article