Bioinspired copper complexes for selective oxidations

Copper-dependent monooxygenase enzymes have gained increasing attention due to their involvement in several areas of biology and chemistry. particulate methane monooxygenase (pMMO) and lytic polysaccharide monooxygenases (LPMO) are included in this category of metalloenzymes that can activate the strong C-H bonds of methane and polysaccharides. We have developed model systems to understand the factors that modulate the properties of the copper centers at these active sites that direct their reactivity for selective C-H activations, controlling the oxidizing power of highly reactive copper-oxygen intermediates. Synthesis and characterization of complexes and reactive intermediates through spectroscopic techniques allowed us to probe these properties. The advancement in this direction with benzimidazole-based ligands as scaffolds to emulate the active site properties and reactivity of copper monooxygenases, their spectroscopic signatures. Emphasis will be placed on the potential applications of these bioinspired systems in catalytic oxidation reactions.