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Elan Zohar Eisenmesser,1Daryl A. Bosco,1Mikael Akke,2Dorothee Kern1*
Internal protein dynamics are intimately connected to
enzymatic catalysis. However, enzyme motions linked to substrate
turnoverremain largely unknown. We have studied dynamics of an enzymeduring catalysis at atomic resolution using nuclear magnetic resonancerelaxation methods. During catalytic action of the enzyme cyclophilinA, we detect conformational fluctuations of the active site thatoccur
on a time scale of hundreds of microseconds. The rates ofconformational dynamics of the enzyme strongly correlate withthe
microscopic rates of substrate turnover. The present results,together
with available structural data, allow a prediction ofthe reaction
trajectory.
1 Department of Biochemistry, Brandeis
University, Waltham, MA 02454, USA.
2 Department of
Biophysical Chemistry, Lund University, Post Office Box 124, SE-221 00 Lund, Sweden.
*
To whom correspondence should be addressed. E-mail:
dkern{at}brandeis.edu
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