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dc.contributor.authorHobbs, Joanne K.
dc.contributor.authorJiao, Wanting
dc.contributor.authorEaster, Ashley Davys
dc.contributor.authorParker, Emily J.
dc.contributor.authorSchipper, Louis A.
dc.contributor.authorArcus, Vickery L.
dc.coverage.spatialUnited Statesen_NZ
dc.identifier.citationHobbs, J. K., Jiao, W., Easter, A. D., Parker, E. J., Schipper, L. A., & Arcus, V. L. (2013). Change in Heat Capacity for Enzyme Catalysis Determines Temperature Dependence of Enzyme Catalyzed Rates. ACS Chemical Biology, published online on September 9 2013.en_NZ
dc.description.abstractThe 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 temperature dependence of ΔG‡ that determines the temperature dependence of enzyme activity. Through mutagenesis, we demonstrate that the Topt of an enzyme is correlated with ΔC‡p and that changes to ΔC‡p are sufficient to change Topt without affecting the catalytic rate. Furthermore, using X-ray crystallography and molecular dynamics simulations we reveal the molecular details underpinning these changes in ΔC‡p. The influence of ΔC‡p on enzymatic rates has implications for the temperature dependence of biological rates from enzymes to ecosystems.en_NZ
dc.publisherAmerican Chemical Societyen_NZ
dc.relation.ispartofACS Chemical Biology
dc.titleChange in heat capacity for enzyme catalysis determines temperature dependence of enzyme catalyzed ratesnzyme Catalyzed Ratesen_NZ
dc.typeJournal Articleen_NZ
dc.relation.isPartOfACS Chemical Biologyen_NZ

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