Characterization of copper intermediates in enzymes and other catalysts that attack strong C-H bonds is important for unraveling oxidation catalysis mechanisms and, ultimately, designing new, more efficient catalytic systems. New insights into the nature of such intermediates may be obtained through the design, synthesis, and characterization of copper-oxygen complexes. Two key proposed examples contain [CuO2]+ and [CuOH]2+ cores, which have been suggested as possible reactive intermediates in monocopper enzymes such as lytic polysaccharide monooxygenase. Recent progress toward the characterization of the structures and properties of complexes with these cores that feature the same supporting ligand will be described, and detailed comparisons of their kinetics in reactions with C-H and O-H bonds will be discussed. Notable differences in their PCET reaction pathways with para-substituted phenols has been discovered that shed new light on the fundamental chemistry of these important core structures.
Proton-Coupled Electron Transfer by Copper-Oxygen Species Relevant to Enzyme Intermediates
Time and Location:
3:30 PM| Mechanical Engineering Building (MEC) Room 205
Friday, November 1, 2019
Professor William Tolman
Washington University in St. Louis
Professor Charlie Machan