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Enzyme dynamics during catalysis.

Authors
Type
Published Article
Journal
Science
1095-9203
Publisher
American Association for the Advancement of Science (AAAS)
Publication Date
Volume
295
Issue
5559
Pages
1520–1523
Identifiers
PMID: 11859194
Source
Medline
License
Unknown

Abstract

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.

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