Functional biomimetics for copper oxidases: interesting catalytic promiscuity of novel monocopper( ii ) complexes

values that are closer to those of the natural enzyme. This is due to the presence of ligand flexibility, structural distortion, an appropriate chelate ring size, a labile donor, a positive redox potential, and a persistent catalyst-substrate interaction. Therefore, the two monocopper(II) complexes serve as the most efficient promiscuous catalysts, acting as complementary agents to the activity of copper oxidase enzymes and superior models for oxidation processes.