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2013 | OriginalPaper | Chapter

Relationship of Femtosecond–Picosecond Dynamics to Enzyme-Catalyzed H-Transfer

Authors : Christopher M. Cheatum, Amnon Kohen

Published in: Dynamics in Enzyme Catalysis

Publisher: Springer Berlin Heidelberg

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Abstract

At physiological temperatures, enzymes exhibit a broad spectrum of conformations, which interchange via thermally activated dynamics. These conformations are sampled differently in different complexes of the protein and its ligands, and the dynamics of exchange between these conformers depends on the mass of the group that is moving and the length scale of the motion, as well as restrictions imposed by the globular fold of the enzymatic complex. Many of these motions have been examined and their role in the enzyme function illuminated, yet most experimental tools applied so far have identified dynamics at time scales of seconds to nanoseconds, which are much slower than the time scale for H-transfer between two heavy atoms. This chemical conversion and other processes involving cleavage of covalent bonds occur on picosecond to femtosecond time scales, where slower processes mask both the kinetics and dynamics. Here we present a combination of kinetic and spectroscopic methods that may enable closer examination of the relationship between enzymatic C–H → C transfer and the dynamics of the active site environment at the chemically relevant time scale. These methods include kinetic isotope effects and their temperature dependence, which are used to study the kinetic nature of the H-transfer, and 2D IR spectroscopy, which is used to study the dynamics of transition-state- and ground-state-analog complexes. The combination of these tools is likely to provide a new approach to examine the protein dynamics that directly influence the chemical conversion catalyzed by enzymes.

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Metadata
Title
Relationship of Femtosecond–Picosecond Dynamics to Enzyme-Catalyzed H-Transfer
Authors
Christopher M. Cheatum
Amnon Kohen
Copyright Year
2013
Publisher
Springer Berlin Heidelberg
DOI
https://doi.org/10.1007/128_2012_407

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