Hydrogen tunneling in enzymes: Linking the role of protein dynamics to catalysis

BIOL 180

Judith P. Klinman, klinman@berkeley.edu, Departments of Chemistry and Molecular and Cell Biology, University of California, Berkeley, 125 Lewis Hall, Berkeley, CA 94720-1460
Data accrued over the last decade and a half point toward the importance of quantum mechanical behavior in enzymatic C-H activation reaction, in particular the phenomenon of hydrogen moving through, rather than over the reaction barrier. Such behavior impacts how we define enzyme catalysis and can provide unique insight into the contributions of motions within the protein environment to catalysis. This presentation will focus on experimental systems that allow correlations to be drawn between protein dynamics and the enzymatically catalyzed chemical conversion step. (Supported by funding from the National Institutes of Health (GM025765) and the National Science Foundation (MCB0446395).
 

Repligen Award Symposium: Enzymatic Catalysis and Transition States
1:30 PM-4:40 PM, Wednesday, 13 September 2006 Moscone Center -- Room 238, Oral

Division of Biological Chemistry

The 232nd ACS National Meeting, San Francisco, CA, September 10-14, 2006