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Reaction kinetics in living systems

H Eyring, S M Ma, I Ueda

    Proceedings of the National Academy of Sciences of the United States of America
    |September 1, 1981
    PubMed
    Summary
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    This study unifies reaction rates, equilibrium, and thermodynamics in biological systems. Enzymes utilize electrostatic polarization and water

    Area of Science:

    • Biophysics
    • Biochemistry
    • Physical Chemistry

    Background:

    • Biological reactions are complex, involving enzymes and proteins.
    • Understanding reaction kinetics and thermodynamics is crucial for biological processes.

    Purpose of the Study:

    • To present reaction rates, equilibrium theory, and irreversible thermodynamics as a unified discipline.
    • To explore the role of enzymes and protein structure in controlling biological reaction rates.
    • To discuss various biological processes through the lens of enzymatic reactions and thermodynamic principles.

    Main Methods:

    • Formalism equating biological networks with electrical and mechanical analogs.
    • Analysis of enzyme-substrate interactions via electrostatic polarization.
    • Investigating the influence of water on reaction rates.

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  • Applying thermodynamic principles to biological processes like luminescence, catalysis, nerve excitation, and anesthesia.

    • Main Results:

    • Enzymes use zwitterions for substrate distortion via electrostatic polarization.
    • Water accelerates reactions by weakening polar bonds.
    • Biological systems exhibit energy consumption and coupling effects.
    • Quenching and unsymmetrical barriers enhance driving force efficiency, akin to transistors.

    Conclusions:

    • Reaction rates, equilibrium, and thermodynamics are interconnected aspects of a single discipline.
    • Enzymatic catalysis and protein structure are key determinants of biological reaction speed.
    • Thermodynamic principles provide a framework for understanding diverse biological phenomena and energy dynamics.