Ubiquitous declines in biochemical reaction rates above optimal temperatures (Topt) are normally attributed to enzyme state changes, but such mechanisms appear inadequate to explain pervasive Topt well below enzyme deactivation temperatures (Tden). Here, a meta-analysis of 92 experimental studies shows that product formation responds twice as strongly to increased temperature than diffusion or transport. This response difference has multiple consequences for biochemical reactions, such as potential shifts in the factors limiting reactions as temperature increases and reaction-diffusion dynamics that predict potential product inhibition and limitation of the reaction by entropy production at temperatures below Tden. Maximizing entropy production by the reaction predicts Topt that depend on enzyme concentration and efficiency as well as reaction favorability, which are patterns not predicted by mechanisms of enzyme state change. However, these predictions are strongly supported by patterns in a meta-analysis of 121 enzyme kinetic studies. Consequently, reaction-diffusion thermodynamics and entropy production may constrain organism performance at higher temperatures, yielding temperature optima of life that may depend on reaction characteristics and environmental features rather than just enzyme state changes.
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