Date of Award
Doctor of Philosophy (PhD)
Metalloenzymes containing copper play a central role in activating dioxygen in biologic systems. Investigations of copper-oxygen intermediates and their catalytic pathways have been of interest. Among the copper enzymes that activate dioxygen to oxidize organic substrates, multicopper oxidase (MCO) are poorly understood due to the lack of synthetic small molecules that model the copper-oxygen intermediates in the MCO catalytic cycle. The goal of this research is to synthesize complexes that model copper-oxygen intermediates in MCO, with particular emphasis on generating and characterizing a (peroxo)copper species analogous to a key proposed active site species in the enzymes. In Chapter 1, proposed copper-oxygen intermediates in copper enzymes are discussed and their spectroscopic properties compared to relevant synthetic model complexes. Chapters 2 and 3 present the reactions of monocopper(II) superoxide and dicopper(I) complexes in efforts to model the MCO peroxo intermediate (PI). In Chapter 4, studies of novel interconversions of (peroxo)copper species are discussed, along with the reactions of monocopper(II) superoxide and monocopper(I) complexes.
Chair and Committee
William B. Tolman
John R. Bleeke, Timothy A. Wencewicz, Richard A. Loomis, Joseph Jez,
Zhong, Xinzhe, "Using Monocopper-Superoxo Complexes in Reactions with Mono- and Dicopper(I) Complexes" (2023). Arts & Sciences Electronic Theses and Dissertations. 2928.
Available for download on Tuesday, May 10, 2095