[MOS] March 4, 2008

[Zina Queen]

Seminar on
Modern Optics and Spectroscopy


Christopher Cheatum,
University of Iowa

Watching the protein mambo:
  Fast enzyme dynamics

March 4, 2008

12:00 - 1:00 p.m.



The structural dynamics of enzymes at the femtosecond to picosecond 
time scale have been invoked to explain the results of 
temperature-dependent kinetic-isotope-effect measurements for a 
number of enzymatic reactions.  We report studies of enzyme-ligand 
interaction dynamics at this time scale.  To identify the residues 
that control the dynamics, we have probed the fluctuations of 
isozymes and mutants of human carbonic anhydrase. We have also 
studied enzyme dynamics in a transition-state-analog complex for the 
enzyme formate dehydrogenase.  Our results support a potential role 
for fast dynamics near the transition state and reveal differences in 
the nature of enzyme-ligand interaction dynamics in the ground state 
and in vicinity of the transition state of a reaction.
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