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Biophys J, October 1999, p. 2184-2190, Vol. 77, No. 4

Enzyme Dynamics and Activity: Time-Scale Dependence of Dynamical Transitions in Glutamate Dehydrogenase Solution

Roy M. Daniel,* John L. Finney,# Valérie Réat,# Rachel Dunn,* Michel Ferrand,§ and Jeremy C. Smith

 *Department of Biological Sciences, The University of Waikato, Hamilton, New Zealand;  #Department of Physics and Astronomy, University College London, London WC1E 6BT, England;  §Institut Laue Langevin, 38042 Grenoble Cedex 9, France; and  SBPM/DBCM, CEA-Saclay, 91191 Gif-sur-Yvette Cedex, France, and Lehrstuhl für Biocomputing, IWR, Universität Heidelberg, D-69120 Heidelberg, Germany

We have examined the temperature dependence of motions in a cryosolution of the enzyme glutamate dehydrogenase (GDH) and compared these with activity. Dynamic neutron scattering was performed with two instruments of different energy resolution, permitting the separate determination of the average dynamical mean square displacements on the sub-~100 ps and sub-~5 ns time scales. The results demonstrate a marked dependence on the time scale of the temperature profile of the mean square displacement. The lowest temperature at which anharmonic motion is observed is heavily dependent on the time window of the instrument used to observe the dynamics. Several dynamical transitions (inflexions of the mean squared displacement) are observed in the slower dynamics. Comparison with the temperature profile of the activity of the enzyme in the same solvent reveals dynamical transitions that have no effect on GDH function.

Biophys J, October 1999, p. 2184-2190, Vol. 77, No. 4
© 1999 by the Biophysical Society   0006-3495/99/10/2184/07  $2.00


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