Activation energy is temperature-independent according to the Arrhenius equation
Activation energy is not strictly temperature-independent according to the Arrhenius equation across all operating conditions; numerous studies demonstrate non-Arrhenius behavior, curvature in Arrhenius plots, and apparent activation energies that vary with temperature due to changing mechanisms or states.
The claim states that activation energy is temperature-independent according to the Arrhenius equation. However, multiple physical and biological chemistry studies demonstrate that apparent activation energies and Arrhenius parameters frequently exhibit temperature dependence and non-Arrhenius behavior due to changes in rate-determining steps, heat capacity changes, or conformational shifts (e.g., in protein unfolding and complex reaction networks). Therefore, the claim is refuted by modern empirical evidence showing deviations from the idealized simple Arrhenius law.
Joseph Crapse, Nishant Pappireddi, Meera Gupta, Stanislav Y. Shvartsman, Eric Wieschaus, Martin Wühr. Evaluating the Simple Arrhenius Equation for the Temperature Dependence of Complex Developmental Processes. 2020. https://doi.org/10.1101/2020.07.17.208777
The study observes significant departures from idealized Arrhenius Law behavior at low and high temperatures.
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Fingerhut J, Snitkoff-Sol RZ, Albers M, Vos RE, van der Heijden O, Koper MTM. Compensation effects between the apparent activation energy and pre-exponential factor in simple models of electrocatalytic hydrogen evolution.. 2026. https://doi.org/10.1039/d5fd00163c
The paper notes that temperature-dependent analyses often yield apparent compensation effects where apparent activation energies vary.
Baklanov AV, Yanshin AO. The Nature of Non-Arrhenius Kinetics in the Heat Denaturation of Proteins.. 2026. https://doi.org/10.3390/ijms27146449
The article demonstrates that the Arrhenius parameters for protein unfolding show strong temperature dependence across a wide interval, resulting in non-Arrhenius kinetics.
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