Herein, is the rate constant, is the reaction temperature, is the universal gas constant and and ℎ are the Boltzmann and Planck constants, respectively. Δ ‡ and Δ ‡ are the enthalpy and entropy change between the reactants and the transition state. The transmission coefficient κ is presumed to be 1 hereafter. Despite this equation holding remarkably well for most chemical transformations, there is a growing consensus that enzyme-catalyzed reactions can deviate from the rate-temperature relationship predicted by the Eyring equation by displaying a curvature in their Eyring plots. This behavior has been shown to originate from a heat capacity change between the enzyme substrate complex and the enzyme transition state complex, caused by preorganization of the enzyme along the reaction coordinate (i.e. during transition state binding). This molecular property has been described by the Macromolecular Rate Theory (MMRT), which extends the Eyring equation by terms accounting for activation heat capacity changes. = ℎ -Δ ‡ -Δ ‡ ( -)