Seminar - Timothy A. Jackson, Stéphane Torelli and Kabibi Kamashanju

Understanding the Function of Manganese-Dependent Enzymes using Bio-inspired Complexes
 
A variety of manganese-dependent enzymes eschew the formation of metal intermediates in high oxidation states and instead rely upon mid-valent manganese(III) centers to promote oxidation-reduction reactions with substrates. Examples include manganese superoxide dismutase and manganese lipoxygenase, which respectively defend organisms from the problematic superoxide radical and promote peroxidation of poly unsaturated fatty acids. In these enzymes, Mn^III-hydroxo and Mn^III-peroxo intermediates commonly perform reactions with substrates. In order to understand the fundamental properties and chemical reactivity of such mid-valent manganese adducts, our lab has generated synthetic models of Mn^III-hydroxo and Mn^III-alkylperoxo intermediates that are amenable to detailed structure-function studies. Using an amide-containing pentadentate ligand, we have generated a family of Mn^III-hydroxo complexes with systematically perturbed geometric and electronic structures. Variations in the primary and secondary coordination spheres of these complexes reveal that reactivity is controlled by an interplay between metal ion reduction potential and ligand basicity. Complementary studies of Mn^III-alkylperoxo adducts highlight differences in reactivity between synthetic and enzymatic intermediates.

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