Less symmetrical dicopper(II) complexes as catechol oxidase models--an adjacent thioether group increases catecholase activity |
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Authors: | Merkel Michael Möller Niclas Piacenza Manuel Grimme Stefan Rompel Annette Krebs Bernt |
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Institution: | Institut für Anorganische und Analytische Chemie der Westf?lischen Wilhelms-Universit?t, Wilhelm-Klemm-Strasse 8, 48149 Münster, Germany. |
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Abstract: | Three new unsymmetrical compartmental dinucleating ligands, 4-bromo-2-(4-methylpiperazin-1-ylmethyl)-6-{2-(1-piperidyl)ethyl}aminomethyl]phenol (HL1), 4-bromo-2-(4-methylpiperazin-1-ylmethyl)-6-{2-(morpholin-4-yl)ethyl}aminomethyl]phenol (HL2), and 4-bromo-2-(4-methylpiperazin-1-ylmethyl)-6-{2-(thiomorpholin-4-yl)ethyl}aminomethyl]phenol (HL3), have been synthesized in order to model the active site of type 3 copper proteins. The dicopper(II) complexes of these ligands give first hints about the influence of a thioether group close to the metal site. The bromophenol-based ligands have one piperazine arm and one other bidentate arm in positions 2 and 6 of the phenolic ring, respectively. With each ligand a dinuclear copper(II) complex was prepared and structurally characterized. The copper ions were found to have square pyramidal environments and a mixture of endogenous phenoxo and exogenous acetate bridging. The influence of a heteroatom in one arm of the ligand on catecholase activity and speciation in solution was studied by UV/Vis spectroscopy, ESI-MS experiments and, DFT calculations. |
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Keywords: | bioinorganic chemistry catechol oxidase copper enzyme models structure–property relationships |
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