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Mathew Vetticatt

Dr. Mathew J. Vetticatt

Assistant Professor of Chemistry

Science 2 Bldg - Room 332
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Research Interests:

My research program utilizes a mechanism-based approach to the rational design of novel reactions in asymmetric organocatalysis (enantioselective catalysis by small organic molecules). Selectivity in asymmetric organocatalysis is often governed by subtle catalyst-substrate interactions. My research group investigates these interactions using a combined experimental and theoretical approach. We employ physical organic probes, such as experimental/theoretical kinetic isotope effects and transition state analysis, as design tools in our studies. We are especially interested in understanding the role of non-conventional hydrogen-bonding interactions such as CH⋅⋅⋅O interactions in determining selectivity in organocatalysis.

My group is also involved in collaborative projects with a number of other synthetic methodology research groups. These collaborations are designed to accelerate methodology development by minimizing the time between reaction discovery and its mechanistic description. Yet another area of focus in my group is mechanistic enzymology and computer-aided drug design. We collaborate with enzymologists to determine the transition state structure of enzymatic reactions and use that information as a blueprint for the rational design of powerful transition state analog inhibitors.

Recent Selected Publications

Vetticatt, M. J.; Itin, B.; Evans, G. B.; Schramm, V. L. Distortional Binding of Transition State Analogues to Human PNP probed by MAS Solid State NMR. Proc. Natl. Acad. Sci. USA. (In Press)

Vetticatt, M. J.; Desai A. A.; Wulff, W. D. Isotope Effects and Mechanism of the Asymmetric BOROX Brønsted Acid Catalyzed Aziridination Reaction. J. Org. Chem. 2013, 78, 5142–5152.

Burgos, E. S.; Vetticatt, M. J.; Schramm, V. L. Recycling Nicotinamide. The Transition-State Structure of Human Nicotinamide Phosphoribosyltransferase. J. Am. Chem. Soc. 2013, 135, 3485–3493.

Vetticatt, M. J.; Singleton, D. A. Isotope Effects and Heavy-Atom Tunneling in the Roush Allylboration of Aldehydes. Org. Lett. 2012, 14, 2370–2373.

Silva, R. G.; Vetticatt, M. J.; Merino, E. F.; Cassera, M. B.; Schramm, V. L. Transition-State Analysis of Trypanosoma cruzi Uridine Phosphorylase-Catalyzed Arsenolysis of Uridine. J. Am. Chem. Soc. 2011, 133, 9923–9931.

Schwartz, P. A.; Vetticatt, M. J.; Schramm, V. L. Transition State Analysis of the Arsenolytic Depyrimidination of Thymidine by Human Thymidine Phosphorylase. Biochemistry 2011, 50, 1412-1420.

Schwartz, P. A.; Vetticatt, M. J.; Schramm, V. L. Transition State Analysis of Thymidine Hydrolysis by Human Thymidine Phosphorylase. J. Am. Chem. Soc. 2010, 132, 13425-13433.

Vetticatt, M. J.; Desai A. A.; Wulff, W. D. How the Binding of Substrates to a Chiral Polyborate Counterion Governs Diastereoselection in an Aziridination Reaction: H-Bonds in Equipoise. J. Am. Chem. Soc. 2010, 132, 13104-13107. Highlighted in 2010 C&EN Volume 88, Issue 37, p. 27.

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Last Updated: 9/4/13