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Related Experiment Videos

Enzyme activity below the dynamical transition at 220 K

R M Daniel1, J C Smith, M Ferrand

  • 1Department of Biological Sciences, University of Waikato, Hamilton, New Zealand.

Biophysical Journal
|October 28, 1998
PubMed
Summary

Enzyme activity does not require anharmonic motion below its dynamical transition temperature. Glutamate dehydrogenase remains active and follows Arrhenius behavior even without detected anharmonic dynamics.

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Area of Science:

  • Biophysics
  • Enzymology
  • Protein Dynamics

Background:

  • Enzyme function is linked to anharmonic motions, but their role in enzyme catalysis remains unclear.
  • A temperature-dependent transition from harmonic to anharmonic motion in proteins is observed, but its connection to enzyme activity is unknown.

Purpose of the Study:

  • To investigate the relationship between protein dynamics and enzyme activity.
  • To determine if the dynamical transition in proteins is essential for enzyme function.

Main Methods:

  • Parallel measurements of glutamate dehydrogenase activity and dynamics using neutron scattering.
  • Analysis of atomic fluctuations faster than 100 ps as a function of temperature.

Main Results:

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  • Glutamate dehydrogenase remains active below its dynamical transition temperature (~220 K).
  • No anharmonic motion was detected below this transition.
  • Enzyme activity showed no significant deviation from Arrhenius behavior down to 190 K.

    • Conclusions:

    • The observed dynamical transition in enzyme motion is decoupled from the rate-limiting step of the reaction.
    • Anharmonic motions are not required for enzyme activity at physiological temperatures above the transition.