The main focus on my research are the antiferromagnetically coupled biniuclear Cu(II) sites of hemocyanin, catechol oxidase, and tyrosinase. The catalytically active metal binding sites of these proteins exhibit similar spectroscopic features, but exhibit different reactivities. Hc reversibly binds molecular oxygen in arthropods and mollusks, and CO binds oxygen and can oxidize o-diphenols (catechols) to their corresponding o-quinones. Ty can perform the same reactions as Hc and CO, and also monooxgenates monophenolic substrates (such as the side chain of Tyrosine) to o-diphenols. The reactive capabilities of these three proteins may derive from differences in protein structures (i.e. limited substrate access to the Cu site) or from electronic structure variations of the Cu-O core. A variety of spectroscopic methods, coupled with QM, MM, and QM/MM computational methods are being used to elucidate the origins of the reactive differences of these proteins.

My Personal Webpage