In this lecture I will discuss recent developments from our lab in the areas of biomimetic metalloporphyrin catalysts and those of novel, heme-thiolate APO biocatalysts with active sites similar to that of cytochrome P450. A perspective of the current state of the field will be presented with connections to key conceptual advances regarding the preparation and characterization of high-valent metal-oxo species and their reactivity. We have directly observed and kinetically characterized the reactive intermediate, « compound I », responsible for C-H hydroxylation by APO enzymes (1,2). Our studies of C-H hydroxylation led to the discovery of a selective and efficient C-H fluorination mediated by a model manganese porphyrin (3,4). The method allows the facile production of fluorinated drug analogs directly from the parent drug. Further, fluorination with 18F sources may allow access to new PET imaging agents. 1. X. Wang, S. Peter, M. Kinne, M. Hofrichter, J. T. Groves, J. Am. Chem. Soc., 2012, 134, 12897. 2. X. Wang, S. Peter, R. Ullrich, M. Hofrichter, J. T. Groves, Angew. Chem. Int. Ed. 2013, 52, 9238. 3. W. Liu, X. Huang, M.-J. Cheng, R. J. Nielsen, W. A. Goddard, III, J. T. Groves, Science, 2012, 337, 1322. 4. X. Huang, W. Liu, H. Ren, R. Neelamegam, J. M. Hooker and J. T. Groves, J. Am. Chem. Soc. 2014, 136, 6842.

Award Address (ACS Award in Inorganic Chemistry sponsored by Aldrich Chemical Co., LLC). Metalloporphyrins in chemical and biological catalysis

249th National Meeting (2015)

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