Change in heat capacity for enzyme catalysis determines temperature dependence of enzyme catalyzed rates.

@article{Hobbs2013ChangeIH,
  title={Change in heat capacity for enzyme catalysis determines temperature dependence of enzyme catalyzed rates.},
  author={Joanne K. Hobbs and Wanting Jiao and Ashley D Easter and Emily J Parker and Louis A Schipper and Vickery L Arcus},
  journal={ACS chemical biology},
  year={2013},
  volume={8 11},
  pages={2388-93}
}
The increase in enzymatic rates with temperature up to an optimum temperature (Topt) is widely attributed to classical Arrhenius behavior, with the decrease in enzymatic rates above Topt ascribed to protein denaturation and/or aggregation. This account persists despite many investigators noting that denaturation is insufficient to explain the decline in enzymatic rates above Topt. Here we show that it is the change in heat capacity associated with enzyme catalysis (ΔC(‡)p) and its effect on the… CONTINUE READING
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