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Science 22 February 2002:
Vol. 295. no. 5559, pp. 1520 - 1523
DOI: 10.1126/science.1066176
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Reports

Enzyme Dynamics During Catalysis

Elan Zohar Eisenmesser,1 Daryl A. Bosco,1 Mikael Akke,2 Dorothee Kern1*

Internal protein dynamics are intimately connected to enzymatic catalysis. However, enzyme motions linked to substrate turnover remain largely unknown. We have studied dynamics of an enzyme during catalysis at atomic resolution using nuclear magnetic resonance relaxation methods. During catalytic action of the enzyme cyclophilin A, we detect conformational fluctuations of the active site that occur on a time scale of hundreds of microseconds. The rates of conformational dynamics of the enzyme strongly correlate with the microscopic rates of substrate turnover. The present results, together with available structural data, allow a prediction of the 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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