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Related Experiment Videos

Quantifying energetic contributions to ground state destabilization.

Vernon E Anderson1

  • 1Department of Biochemistry, Case Western Reserve University, 10900 Euclid Avenue, Cleveland, OH 44106-4935, USA. vea@case.edu

Archives of Biochemistry and Biophysics
|December 8, 2004
PubMed
Summary
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Enzyme active sites polarize substrate bonds upon binding, altering vibrational frequencies. This bond polarization, quantified by quantum chemistry, leads to equilibrium isotope effects, clarifying substrate activation in catalysis.

Area of Science:

  • Biochemistry
  • Chemical Physics
  • Enzyme Kinetics

Background:

  • Substrate binding to enzyme active sites often induces significant bond polarization.
  • This polarization arises from desolvation, conformational changes, and electric field effects within the active site.

Purpose of the Study:

  • To quantify the extent of bond polarization during substrate-enzyme association.
  • To understand the relationship between bond polarization, vibrational frequency shifts, and equilibrium isotope effects.
  • To elucidate the role of substrate activation in enzyme catalysis.

Main Methods:

  • Utilizing vibrational spectroscopy to identify bond polarization.
  • Employing quantum chemical calculations to quantify polarization in terms of partial charge and energy.

Related Experiment Videos

  • Analyzing changes in vibrational frequencies during substrate binding.

    • Main Results:

    • Vibrational spectroscopy confirmed significant bond polarization upon substrate association.
    • Quantum chemical calculations provided quantitative measures of polarization and its energetic contribution.
    • Observed changes in vibrational frequencies directly correlate with equilibrium isotope effects on association.

    Conclusions:

    • Bond polarization is a key event in substrate-enzyme interactions.
    • Equilibrium isotope effects are a consequence of vibrational frequency changes during binding.
    • Understanding these molecular changes enhances our knowledge of enzyme catalytic mechanisms and substrate activation.