The active sites in dioxygenase proteins degrade heteroaromatic substrates into aliphatic compounds by incorporating molecular oxygen. Quercetin 2,3 dioxygenase (QDO) is the only definitively characterized copper-containing protein in this class. Although the mechanism of QDO degradation is not well understood, several model complexes have been studied that mimic the reactivity and coordination of the native enzyme active site. Structurally the majority of these models demonstrate bidentate coordination of the copper center with the quercetin, forming a stable, five-membered chelate ring. The bidentate coordination differs from the monodentate coordination in the native enzyme making the complexes less viable as models for dioxygenase. We propose a monodentate model that mimics the geometric arrangement of the QDO active site. Density functional theory studies will elucidate the comparative energetics of monodentate and bidentate models, as well as the effect of the energetics on the reactivity. 

Model complex computational investigations of the copper dioxygenase active site

243rd National Meeting (2012)

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