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Solvent structure and enzyme activity.

J R Brorson1, E S Novak, M W Makinen

  • 1Department of Biophysics and Theoretical Biology, University of Chicago, Cummings Life Science Center, Illinois 60637.

Journal of Biomolecular Structure & Dynamics
|August 1, 1985
PubMed
Summary
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Enzyme activity is not significantly affected by solvent structure changes, even with strong water-perturbing solutes. Enzyme fluctuations crucial for catalysis are independent of bulk solvent dynamics in low viscosity environments.

Area of Science:

  • Biochemistry
  • Physical Chemistry
  • Enzyme Kinetics

Background:

  • Enzymes exist in thermal equilibrium with their solvent environment.
  • Models suggest enzyme catalysis relies on vibrational modes or catalytic group motion triggered by solvent interactions.
  • Solvent composition and structure are hypothesized to influence these enzyme-solvent interactions.

Purpose of the Study:

  • To investigate the influence of solvent structure and composition on enzyme catalytic activity.
  • To determine if strong water-structure-perturbing solutes affect enzyme kinetics.
  • To examine the relationship between bulk solvent dynamics and enzyme structural fluctuations in catalysis.

Main Methods:

  • Enzyme kinetics of carboxypeptidase A and alpha-chymotrypsin were measured.

Related Experiment Videos

  • Aqueous mixtures containing perturbing solutes (p-dioxane, t-butanol, tetraalkylammonium chlorides) were used as solvents.
  • Kinetic parameters were analyzed in relation to solvent composition and structure.

    • Main Results:

    • No significant influence of solvent structure or mass composition on the catalytic rate constant was observed for either enzyme.
    • The kinetic parameters remained largely unaffected despite the use of strong water-structure-perturbing solutes.
    • Enzyme structural fluctuations involved in the rate-limiting step were not significantly influenced by bulk solvent dynamics.

    Conclusions:

    • Solvent structure and composition do not play a significant role in the catalytic activity of carboxypeptidase A and alpha-chymotrypsin.
    • The dynamic processes within the bulk solvent do not appear to influence the enzyme's internal fluctuations critical for catalysis.
    • These findings challenge models that emphasize solvent-mediated dynamics as the primary driver of enzyme catalytic activity.