This research employs the principles of bioinorganic modeling, simplifying the extraneous structures of the molecule being mimicked and focusing only on the active components of the large biological molecules. Specifically, this project attempts to mimic the structure and reactivity of tri-copper active sites found in Multi-copper Oxidises, such as Laccase and Ceruloplasmin, that bind with oxygen and reduce it to water. After experimenting with various other structures that failed to mimic the active sites, we selected another potential ligand, 1,3,5-tri(2-pyridylmethyltriazole)-2,4,6-triethyl benzene, abbreviated Ltapma, to be the substrate for this research to bind with three Cu(I) ions and then to bind with oxygen molecules. Our immediate goal for this research is to synthesize and purify the proposed ligand, and bind it to Cu(I) ions to obtain the crystal structure of the tri-copper complex. If possible, we would also like to have this complex bind with oxygen and study the resulting complex. We hope this complexes could emulate the structure and behavior of the tri-copper active sites, and by studying these structures and binding patterns researchers could deduce the mechanism by which the active sites bind to oxygen and, from there, move on to speculating the oxygen reducing mechanism. All these mechanisms could hopefully provide valuable insights into the study of the Wilson’s disease, which occurs when copper-containing oxidases in the human body become defective and lose the ability to bind with copper, and contribute to finding a cure for it.
Wang, Haosen, "Synthesis and Characterization of a Biometric Model of the Tricopper Binding Site of Multicopper Oxidases" (2013). Honors Theses. 25.