Cytochrome c oxidase (CcO), the terminal electron acceptor of the electron transport chain, reduces oxygen (O2) to water (H2O) through the transfer of four electrons and the translocation of four protons across the membrane. Proton movement is responsible for the formation of an electrochemical gradient that can subsequently be dissipated for the formation of ATP. The O2 binding and reduction site in CcO is comprised of metal centers lying adjacent to one another, heme-a3 and CuB. Important high-valent iron-oxo intermediates such as compound I and II in P450 enzymes are strong oxidizing agents capable of C–H bond activation. Such transient intermediates are derived from the binding of O2 to the heme site of the P450 enzyme and scission of the O–O bond along the path towards the reduction of O2 to water and substrate oxidation. Generation of synthetic analogues of compound I and II requires strong oxidants such as m-CPBA or idosobenzene. Synthetic models of CcO were previously shown to oxidize nitric oxide (NO) to nitrite (NO2-). Here, we attempt the generation of compound I and II-type intermediates using mild oxidizing agents for the catalytic oxidation of a variety of substrates. Our mechanistic studies of these synthetic ferryl intermediates will be also discussed.

Heme/Cu model complexes: Oxidative chemistry with mild oxidants

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.