Thiomethyl Substituted Dicopper Complexes: Attempts to Reproduce the Asymmetry of the Active Site from Type 3 Copper Enzymes - Université de Lorraine
Journal Articles Journal of Inorganic and General Chemistry / Zeitschrift für anorganische und allgemeine Chemie Year : 2013

Thiomethyl Substituted Dicopper Complexes: Attempts to Reproduce the Asymmetry of the Active Site from Type 3 Copper Enzymes

Abstract

Two new dinucleating phenol-based ligands (m-HLSMe and p-HLSMe) bearing pyridine-containing pendant arms with a SMe group on one pyridine (meta or para position relative to the pyridine nitrogen atom) have been synthesized. After coordination by two copper(II) ions, the corresponding mu-phenoxido, mu-hydroxido dicopper(II) complexes were isolated and characterized by UV/Vis, EPR spectroscopy, single-crystal X-ray analysis (for the complex with the SMe substituent at the meta position) and electrochemistry. The presented compounds mimic the active site of type 3 copper enzymes and in particular the distinct environments of the copper ions. Both complexes are active as catalysts for the oxidation of 3,5-di-tert-butylcatechol to the respective quinone. The catalytic properties of the complexes depend on substrate binding, as reflected by the K-M values determined for the complexes in presence of 3,5-dtbc and are not correlated directly with the redox properties of the dicopper center.

Dates and versions

hal-01494083 , version 1 (22-03-2017)

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Cite

Wassim Rammal, Katalin Selmeczi, Christian Philouze, Eric Saint-Aman, Jean-Louis Pierre, et al.. Thiomethyl Substituted Dicopper Complexes: Attempts to Reproduce the Asymmetry of the Active Site from Type 3 Copper Enzymes. Journal of Inorganic and General Chemistry / Zeitschrift für anorganische und allgemeine Chemie, 2013, 639 (8-9, SI), pp.1477-1482. ⟨10.1002/zaac.201300059⟩. ⟨hal-01494083⟩
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