Category:
Research Papers
Date Published:
November 28, 2025
Keywords:
rate constant; reactant; activated complex; Equilibrium constant; law of mass action; rate of reaction; Eyring Equation; rate law
Abstract:
This study bridges the gap between chemical kinetics and thermodynamics by developing unified expressions that connect reaction rate laws, temperature dependence, and activation parameters. Using rate equations for both simple and complex reactions, it incorporates stoichiometric coefficients, Arrhenius relations, and Gibbs free energy changes to describe how reaction velocity varies with concentration and temperature. These principles are extended through Transition State Theory (TST), relating the rate constant to kinetic and thermodynamic quantities. The analysis is further applied to enzyme catalysis, deriving rate equations that account for inhibition and show how product formation depends on the rates of enzyme–substrate complex formation and dissociation. The equations also incorporate the standard Gibbs free energy of activation, linking molecular energetics to reaction rates. Overall, this work provides a unified framework for understanding the kinetic and thermodynamic factors that govern chemical reactivity in both simple and complex catalytic systems.
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