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Dynamical origins of heat capacity changes in enzyme-catalysed reactions

Research output: Contribution to journalArticle

Original languageEnglish
Article number1177
Number of pages7
JournalNature Communications
Volume9
Issue number1
DOIs
DateAccepted/In press - 23 Feb 2018
DatePublished (current) - 21 Mar 2018

Abstract

Heat capacity changes are emerging as essential for explaining the temperature dependence of enzyme-catalysed reaction rates. This has important implications for enzyme kinetics, thermoadaptation and evolution, but the physical basis of these heat capacity changes is unknown. Here we show by a combination of experiment and simulation, for two quite distinct enzymes (dimeric ketosteroid isomerase and monomeric alpha-glucosidase), that the activation heat capacity change for the catalysed reaction can be predicted through atomistic molecular dynamics simulations. The simulations reveal subtle and surprising underlying dynamical changes: tightening of loops around the active site is observed, along with changes in energetic fluctuations across the whole enzyme including important contributions from oligomeric neighbours and domains distal to the active site. This has general implications for understanding enzyme catalysis and demonstrating a direct connection between functionally important microscopic dynamics and macroscopically measurable quantities.

    Structured keywords

  • BcompB
  • BrisSynBio
  • Bristol BioDesign Institute

    Research areas

  • Synthetic Biology

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