The catalytic mechanism of dioxygenase enzymes, such as the metalloenzyme quercetin 2, 3, dioxygenase (QDO), which catalyzes the oxidation of two carbon-carbon bonds of quercetin and releases carbon monoxide and the corresponding depside, is not well understood. This project involves the development, synthesis, and characterization of new biomimetic model systems consisting of a tetra-dentate N3O–containing ligand (BPG) and divalent first-row transition metal ions observed in bacterial and fungal QDO enzymes. The goal of this research is to understand how the unique active site of this enzyme cleaves the O-heterocyclic ring of quercetin by evaluating the functionality of a series of metal complexes with ligand systems similar in structure to the active site of QDO. Four metal complexes, [Co(BPG)]+1, [Cu(BPG)]+1, [Zn(BPG)]+1, and [Mn(BPG)]+1, have been isolated, as well as two substrate enzyme model complexes which mimic the QDO active site, [Cu(BPG)(Maltol)], and [Co(BPG)(Maltol)]. This poster will also report preliminary reactivity experiments with O- and N-heterocyclic compounds.

Synthesis, characterization, and applicability of reactive biomimetic model complexes toward important biological reactions

249th National Meeting (2015)

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