Molecular Modeling of Multicopper Oxidases: The Binding of O2 to a Tri-Copper Active Site

Bioinorganic chemistry is the study of inorganic elements in biological systems. One such example of a system can be found in the active site of enzymes, where clusters of metals are chemically responsible for biological reactions. Specifically, this research focuses on multicopper oxidases-enzymes that possess a tri-copper cluster in the active site with the purpose of reducing dioxygen to water, among other reactions. The method of biomimetics is employed, which simplifies researching the tri-copper-oxygen binding mechanism. In using this method, ligand scaffolds are synthesized that mimic the enzyme\u27s active site and therefore reduce the complexity of the studied reaction by removing the bulk of the enzyme. Various ligand scaffolds have been synthesized and characterized, but none to date have perfectly modeled a multicopper oxidase after copper(I) was added to the system. The purpose of this research then was to attempt synthesizing a new ligand scaffold for characterization, ultimately with the hope of correctly mimicking a multicopper oxidase. If the molecular model successfully reflects a multicopper oxidase, all research of the binding mechanism would go toward finding a treatment for Wilson disease, which occurs in multicopper oxidases that have become defective in humans, causing illness or even death