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• W2061864005 abstract "The series of compounds [Mn(bpia)(μ-OAc)]2(ClO4)2 (1), [Mn2(bpia)2(μO)(μ-OAc)](ClO4)3·CH3CN (2), [Mn(bpia)(μ-O)]2(ClO4)2(PF6)·2CH3CN (3), [Mn(bpia)(Cl)2](ClO)4 (4), and [(Mn(bpia)(Cl))2(μ-O)](ClO4)2·2CH3CN (5) (bpia = bis(picolyl)(N-methylimidazol-2-yl)amine) represents a structural, spectroscopic, and functional model system for manganese catalases. Compounds 3 and 5 have been synthesized from 2 via bulk electrolysis and ligand exchange, respectively. All complexes have been structurally characterized by X-ray crystallography and by UV−vis and EPR spectroscopies. The different bridging ligands including the rare mono-μ-oxo and mono-μ-oxo-mono-μ-carboxylato motifs lead to a variation of the Mn−Mn separation across the four binuclear compounds of 1.50 Å (Mn2II,II = 4.128 Å, Mn2III,III = 3.5326 and 3.2533 Å, Mn2III,IV = 2.624 Å). Complexes 1, 2, and 3 are mimics for the Mn2II,II, the Mn2III,III, and the Mn2III,IV oxidation states of the native enzyme. UV−vis spectra of these compounds show similarities to those of the corresponding oxidation states of manganese catalase from Thermus thermophilus and Lactobacillus plantarum. Compound 2 exhibits a rare example of a Jahn−Teller compression. While complexes 1 and 3 are efficient catalysts for the disproportionation of hydrogen peroxide and contain an N4O2 donor set, 4 and 5 show no catalase activity. These complexes have an N4Cl2 and N4OCl donor set, respectively, and serve as mimics for halide inhibited manganese catalases. Cyclovoltammetric data show that the substitution of oxygen donor atoms with chloride causes a shift of redox potentials to more positive values. To our knowledge, complex 1 is the most efficient binuclear functional manganese catalase mimic exhibiting saturation kinetics to date." @default.
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• W2061864005 date "2002-09-17" @default.
• W2061864005 modified "2023-10-16" @default.
• W2061864005 title "Preparation of Highly Efficient Manganese Catalase Mimics" @default.
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• W2061864005 doi "https://doi.org/10.1021/ic025897a" @default.
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