Metalloenzymes containing Fe and Cu active sites can activate either O2 or N2O to perform difficult but important chemical transformations. Fe and Cu methane monooxygenases use O2 to oxidize CH4 to CH3OH, binuclear copper enzymes reversibly bind O2 and activate it for electrophilic aromatic substitution reactions, and Cu nitrous oxide reductase uses a tetranuclear Cu cluster to carry out the two-electron reduction of N2O to form N2 and H2O. This presentation will cover recent efforts to develop a heterogeneous catalytic approach to carrying out these types of metalloprotein-mediated chemical transformations. In particular, zeolitic superstructures provide a robust architecture for generating and studying highly reactive species, which can be directly compared to parallel sites in biology. Through comparisons made with Fe- and Cu-ZSM-5, we have obtained insights into the similarities and differences between their active site geometric and electronic structures. These insights relate to their ability to activate O2 and/or N2O and their subsequent selective oxidation of CH4.

O2 and N2O activation in transition metal containing zeolites: Comparing heterogeneous and enzymatic catalysis

248th National Meeting (2014)

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