Research Commons
      • Browse 
        • Communities & Collections
        • Titles
        • Authors
        • By Issue Date
        • Subjects
        • Types
        • Series
      • Help 
        • About
        • Collection Policy
        • OA Mandate Guidelines
        • Guidelines FAQ
        • Contact Us
      • My Account 
        • Sign In
        • Register
      View Item 
      •   Research Commons
      • University of Waikato Research
      • Science and Engineering
      • Science and Engineering Papers
      • View Item
      •   Research Commons
      • University of Waikato Research
      • Science and Engineering
      • Science and Engineering Papers
      • View Item
      JavaScript is disabled for your browser. Some features of this site may not work without it.

      Enzyme activity below the dynamical transition at 220 K

      Daniel, Roy M.; Smith, Jeremy C.; Ferrand, Michel; Hery, Stephanie; Dunn, Rachel V.; Finney, John L.
      Thumbnail
      Files
      Biophy Enzyme.pdf
      41.25Kb
      Link
       www.biophysj.org
      Find in your library  
      Citation
      Export citation
      Daniel, R. M., Smith, J. C., Ferrand, M., Hery, S., Dunn, R. & Finney, J.L. (1998). Enzyme activity below the dynamical transition at 220 K. Biophysical Journal, 75(5), 2504- 2507
      Permanent Research Commons link: https://hdl.handle.net/10289/1285
      Abstract
      Enzyme activity requires the activation of anharmonic motions, such as jumps between potential energy wells. However, in general, the forms and time scales of the functionally important anharmonic dynamics coupled to motion along the reaction coordinate remain to be determined. In particular, the question arises whether the temperature-dependent dynamical transition from harmonic to anharmonic motion in proteins, which has been observed experimentally and using molecular dynamics simulation, involves the activation of motions required for enzyme function. Here we present parallel measurements of the activity and dynamics of a cryosolution of glutamate dehydrogenase as a function of temperature. The dynamical atomic fluctuations faster than ~100 ps were determined using neutron scattering. The results show that the enzyme remains active below the dynamical transition observed at ~220 K, i.e., at temperatures where no anharmonic motion is detected. Furthermore, the activity shows no significant deviation from Arrhenius behavior down to 190 K. The results indicate that the observed transition in the enzyme's dynamics is decoupled from the rate-limiting step along the reaction coordinate.
      Date
      1998-11
      Type
      Journal Article
      Rights
      This article has been published in the journal: Biophysical Journal. Copyright © 1998 by the Biophysical Society.
      Collections
      • Science and Engineering Papers [3121]
      Show full item record  

      Usage

      Downloads, last 12 months
      67
       
       

      Usage Statistics

      For this itemFor all of Research Commons

      The University of Waikato - Te Whare Wānanga o WaikatoFeedback and RequestsCopyright and Legal Statement