Articles | Volume 21, issue 5
https://doi.org/10.5194/bg-21-1061-2024
https://doi.org/10.5194/bg-21-1061-2024
Research article
 | 
04 Mar 2024
Research article |  | 04 Mar 2024

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

Jinyun Tang and William J. Riley

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Cited articles

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Alster, C. J., Baas, P., Wallenstein, M. D., Johnson, N. G., and von Fischer, J. C.: Temperature Sensitivity as a Microbial Trait Using Parameters from Macromolecular Rate Theory, Front. Microbiol., 7, 1821, https://doi.org/10.3389/fmicb.2016.01821, 2016. 
Alster, C. J., von Fischer, J. C., Allison, S. D., and Treseder, K. K.: Embracing a new paradigm for temperature sensitivity of soil microbes, Glob. Change Biol., 26, 3221–3229, https://doi.org/10.1111/gcb.15053, 2020. 
Alvarez, G., Shahzad, T., Andanson, L., Bahn, M., Wallenstein, M. D., and Fontaine, S.: Catalytic power of enzymes decreases with temperature: New insights for understanding soil C cycling and microbial ecology under warming, Glob. Change Biol., 24, 4238–4250, https://doi.org/10.1111/gcb.14281, 2018. 
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Short summary
A chemical kinetics theory is proposed to explain the non-monotonic relationship between temperature and biochemical rates. It incorporates the observed thermally reversible enzyme denaturation that is ensured by the ceaseless thermal motion of molecules and ions in an enzyme solution and three well-established theories: (1) law of mass action, (2) diffusion-limited chemical reaction theory, and (3) transition state theory.
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