Exploration of Chemical and Biochemical Mechanisms of Catalysis




Cormier, Kevin William

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Nature uses proteins to catalyze a wide range of chemical processes that control cellular signaling. One such enzyme is ERK2 which plays a role in the transmission of signals by catalyzing the phosphorylation of its substrates. The signaling pathway that it is a part of is important in the control of growth, cell survival and differentiation. As with other proteins, its function is intimately related to its structure, both its activity and selectivity for binding partners affected by its conformation. A mutant of ERK2, discovered in a human oral squamous cell carcinoma cell line, consists of a substitution of a lysine for a glutamic acid residue in the common docking domain (E320K). The effects of this mutation on the structure of ERK2 are examined along with the effect that the conformational change has on protein-protein interactions. Because of the essential role catalysts play in lowering the activation barriers of otherwise inaccessible reaction pathways, chemists have long looked to nature for inspiration. The functionalization of C–H bonds is one such area of research, where the coveted exploitation of readily available hydrocarbon feedstock is impeded by the stability of the bonds. In this search for potential catalysts, chemists have looked to the metals that act as co-factors for many enzymes. Vanadium, long thought to be at work in halogenation reactions taking place in marine environments, was found to selectively catalyze the oxidation of hydrocarbons at the benzylic position. Understanding the mechanism of a reaction can lead to insights into ways to better harness reactivity and selectivity, something that nature does quite efficiently. In studying the biosynthesis of pyrrole-imidazole alkaloids, a means to mimic nature’s method for the dimerization of oroidin was achieved and the product outcome controlled.

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