Reply to Comment on: “Computer Simulations Reveal an Entirely Entropic Activation Barrier for the Chemical Step in a Designer Enzyme”

Åqvist, Johan

doi:10.1021/acscatal.3c02639

ACS Catal.

2023

DOI: 10.1021/acscatal.3c02639

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Reply to Comment on: “Computer Simulations Reveal an Entirely Entropic Activation Barrier for the Chemical Step in a Designer Enzyme”

Johan Åqvist

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2024

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A chemical kinetics theory for interpreting the non-monotonic temperature dependence of enzymatic reactions

Tang,

Riley

2024

Biogeosciences

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Abstract. One notable observation of enzymatic chemical reactions is that, for a given abundance of enzymes and substrates, temperature increases cause reaction rates to first increase consistent with the Arrhenius relationship, then plateau, and finally fall off quickly to zero at high temperatures. While many mathematical functions have been used to describe this pattern, we here propose a chemical kinetics theory which successfully replicates this observation and provides insights into the processes responsible for these dynamics. The chemical kinetics theory combines the law of mass action, von Smoluchowski's diffusion-limited chemical reaction theory, and Eyring's transition state theory. This new theory reveals that the thermally reversible enzyme denaturation ensured by the ceaseless thermal motion of molecules and ions in an enzyme solution explains the plateau and subsequent decrease in chemical reaction rates with increasing temperature. The temperature-dependent affinity parameter (K) that relates enzymes and substrates through their binding also affects the shape of the emergent temperature response. We demonstrate that with an increase in substrate availability, K shifts the optimal temperature, where reaction rates plateau, towards higher values. Further, we show that the chemical kinetics theory accurately represents 12 sets of published enzyme assay data and includes the popular mechanistic model by Ratkowsky et al. (2005) as a special case. Given its good performance and solid theoretical underpinning, we believe this new theory will facilitate the construction of more mechanistic-based environmental biogeochemical models.

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A chemical kinetics theory for interpreting the non-monotonic temperature dependence of enzymatic reactions

Tang,

Riley

2024

Biogeosciences

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Reply to Comment on: “Computer Simulations Reveal an Entirely Entropic Activation Barrier for the Chemical Step in a Designer Enzyme”

Cited by 1 publication

References 12 publications

A chemical kinetics theory for interpreting the non-monotonic temperature dependence of enzymatic reactions

A chemical kinetics theory for interpreting the non-monotonic temperature dependence of enzymatic reactions

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