The coupled binuclear copper enzyme family is responsible for a variety of biological functions including oxygen transport (hemocyanin), substrate oxidation (catechol oxidase), and substrate oxygenation (tyrosinase and the recently discovered hydroxyanilinase). Spectroscopic characterization of the oxy forms of these enzymes indicates they coordinate dioxygen in an indistinguishable fashion despite performing different biological functions. While the active site of hemocyanin is generally not accessible to substrate molecules, catechol oxidase, tyrosinase, and hydroxyanilane catalyze different reactions with similarly sized substrates. Insight into the mechanisms and differential reactivity of these classes of enzymes will be discussed in the context of recent spectroscopic, kinetic, and computational results on these enzymes.

Structure/function correlations in the coupled binuclear copper enzyme family

248th National Meeting (2014)

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