The heat released during catalytic turnover enhances the diffusion of an enzyme

Clement Riedel, Ronen Gabizon, Christian A.M. Wilson, Kambiz Hamadani, Konstantinos Tsekouras, Susan Marqusee, Steve Pressé, Carlos Bustamante

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113 Scopus citations

Abstract

Recent studies have shown that the diffusivity of enzymes increases in a substrate-dependent manner during catalysis1,2. Although this observation has been reported and characterized for several different systems3-10, the precise origin of this phenomenon is unknown. Calorimetric methods are often used to determine enthalpies from enzyme-catalysed reactions and can therefore provide important insight into their reaction mechanisms11,12. The ensemble averages involved in traditional bulk calorimetry cannot probe the transient effects that the energy exchanged in a reaction may have on the catalyst. Here we obtain single-molecule fluorescence correlation spectroscopy data and analyse them within the framework of a stochastic theory to demonstrate a mechanistic link between the enhanced diffusion of a single enzyme molecule and the heat released in the reaction. We propose that the heat released during catalysis generates an asymmetric pressure wave that results in a differential stress at the protein-solvent interface that transiently displaces the centre-of-mass of the enzyme (chemoacoustic effect). This novel perspective on how enzymes respond to the energy released during catalysis suggests a possible effect of the heat of reaction on the structural integrity and internal degrees of freedom of the enzyme.

Original languageEnglish (US)
Pages (from-to)227-230
Number of pages4
JournalNature
Volume517
Issue number7533
DOIs
StatePublished - Jan 8 2015

ASJC Scopus subject areas

  • General

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    Riedel, C., Gabizon, R., Wilson, C. A. M., Hamadani, K., Tsekouras, K., Marqusee, S., Pressé, S., & Bustamante, C. (2015). The heat released during catalytic turnover enhances the diffusion of an enzyme. Nature, 517(7533), 227-230. https://doi.org/10.1038/nature14043