Dr. Vincenzo Venditti, ISU
Host: Dr. Sadow
In my laboratory we use NMR combined with other biophysical and biochemical tools to reveal how the complex interplay between cofactor/substrate binding and conformational dynamics regulates the activity high molecular weight enzymes that are essential for human and bacterial metabolism. We are particularly interested in Enzyme I (EI) of the bacterial phosphotransferase system (PTS), and the human RNA demethylases FTO and Alkbh5. In this seminar I will discuss how conformational disorder plays a crucial role in regulation of these slow enzymes and can be exploited to develop novel strategies for their selective inhibition.
In an extension of this work, we explore the ability of Surface Contrast (SC) NMR techniques, developed recently to probe the binding of small proteins to large molecular machines, aggregates, and nanoparticles, to elucidate the regulatory role of sorption equilibria in heterogeneous catalysis. The approach is illustrated by the phenol hydrogenation reaction catalyzed by ceria-supported palladium nanoparticles. We show that SC-NMR experiments provide unprecedented, atomic-resolution details on the adsorption/desorption equilibria at the surface of the NP catalyst, reporting on the structure, dynamics, and thermodynamics of the adsorbed species. Combined analysis of SC-NMR and reaction kinetics data returns important mechanistic information on the catalytic process, such as the involvement of the ceria support in catalysis.
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