CAREER: Protein dynamics and hydrogen tunneling in enzymatic catalysis

University Of Iowa, Iowa City IA

Investigators

Abstract

Dr. Amnon Kohen of the University of Iowa is funded for his research on protein dynamics and hydrogen tunneling in enzymatic catalysis by a CAREER grant in the Physical Chemistry program of the Chemistry Division. He will develop mechanistic models for how biologically significant C-H bond activation occurs and for the role of protein dynamics, coupled motion, and quantum mechanical hydrogen tunneling in enzyme catalysis. Kinetic isotope effects and temperature effects will be used to probe tunneling and associated reaction mechanism questions. Dr. Kohen will incorporate aspects of bioorganic chemistry, physical organic chemistry, and computational chemistry into the organic laboratory for majors. A new graduate course, Chemical Catalysis in Biology, will be developed and based on recent literature. Enzyme catalysis is one of the most important biochemical phenomena, since it is at the heart of nearly all of our physiological biochemistry (how our food is digested, how our cells reproduce, how hormones induce changes in our body functions, etc.). The role of coupled motion and quantum mechanical hydrogen tunneling in enzyme catalysis will be discerned. Tunneling is the phenomenon by which a molecule or group of reacting molecules transfers through a reaction energy barrier due to its wave-like property. Synchronous motion or coupled motion of atoms in a reacting molecule is a phenomenon that has been found to be important in some enzyme catalyzed reactions. The small but important enzyme, dihydrofolate reductase, that catalyzes hydrogen transfer will be a focal point of this research. Dr. Kohen plans on developing new course work in the area of bioinorganic chemistry for both undergraduate and graduate students.