Aromatic Peroxygenases (APO) are a novel class of heme-thiolate enzymes with extraordinary reactivity toward C-H bonds to afford alcohol products.  The generation and kinetic characterization of the reactive ferryl intermediates of APO will be described. These hydroxylation reactions and their mechanisms will be compared and contrasted to C-H fluorination reactions we have discovered recently using synthetic manganese porphyrins as catalysts.Xiaoshi Wang, Sebastian Peter, Matthias Kinne, Martin Hofrichter, John T. Groves Detection and Kinetic Characterization of a Highly Reactive Heme�Thiolate Peroxygenase Compound I  J. Am. Chem. Soc., 2012 , 134, 12897�12900.Wei Liu, Xiongyi Huang, Mu-Jeng Cheng, Robert J. Nielsen, William A. Goddard, III, John T. Groves,  Oxidative Aliphatic C-H Fluorination with Fluoride Ion Catalyzed by a Manganese Porphyrin, Science, 2012 , 337, 1322-1325.

C-H activation by heme-thiolate proteins and metalloporphyrin catalysts: From hydroxylation to fluorination

245th National Meeting (2013)

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