Mimicking Copper Sites of pMMO via endo- and exo-Functionalized Cage-Compounds

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The depletion of resources, energy supply problems and climate change are major challenges today. Catalysis is believed to be a key aspect in solving these and other urgent problems. Among the desirable transformation, many are known to be mediated by enzymes, natures catalysts. The conversion of methane to methanol is very important from a climatic, scientific and economic point of view. This transformation has so far not sufficiently been mastered by synthetic catalysts. Nature developed two enzyme families that are based on iron and copper, the methane monooxygenases. In particular, little is known about how the more powerful copper-based methane monooxygenases work. One way for a better understanding of enzymes is the development of synthetic model complexes that mimic the structure and functionality of the enzyme of interest. The project aim is to mimic the presumably active sites of the copper-based methane monooxygenase with the goal to understand more of this very important class of metalloenzymes. The approach to achieve this uses functionalized cage compounds that resemble the coordinating amino acid residues of the enzyme in their inner. One goal of the project is to shine light on the role of different copper sites within the copper-based methane monooxygenase. In particular, the projects aim to obtain a better understanding how oxygen and substrate activation occurs within these enzymes active site mimics. A better understanding of the copper-based methane monooxygenases can lead to more powerful catalysts for the conversion of methane to methanol.