Solid State and Solution Characterization of Copper and Cobalt Complexes with Amide and Thioamide Ligands

Abstract

Low molecular weight ligands have been extremely useful for mimicking active intermediates. While often times these low molecular weight compounds are synthesized with ligands that do not always fully mirror the active site, they do hold an advantage over studying intermediates of full proteins due to the complexity of an entire protein. This work utilizes biologically relevant amide groups to explore biomimetic copper chemistry. The amide functional group is found in all biological systems because it forms the peptide backbone. The amide complexes synthesized were studied in terms of electronic ground states, as well as reactivity with biologically relevant oxidants. One dicopper (II:II) amide macrocyclic complex was synthesized and characterized and has shown that the copper centers couple in a ferromagnetic manner. This complex also showed a significant change in the UV-vis spectrum in the presence of potassium superoxide. In future work, this could lend insight into the role and function of prion protein (PrP), a multinuclear copper protein, whose function is still debated in the literature.