The journal club is intended to be a weekly natter about interesting recent research. We tend to stick to high-impact journals - Nature, Science, PNAS and PRL have been popular - but this is not prescriptive. Given the diversity of research in the CM group, chosen topics vary widely. Anyone and everyone is welcome: if you have a paper you want to discuss, email it to me (Joe Tavacoli
) and I'll slot you in.
Week beginning 4 October 2015
Tuesday 6 Oct 15 - 11:30am
To be confirmed
Friday 9 Oct 15 - 11:30am - JCMB 2511
The heat released during catalytic turnover enhances the diffusion of an enzyme
Authors: Clement Riedel, Ronen Gabizon, Christian A. M. Wilson, Kambiz Hamadani, Konstantinos Tsekouras, Susan Marqusee, Steve Pressé & Carlos Bustamante
Speaker: Aidan Brown
Recent studies have shown that the diffusivity of enzymes increases in a substrate-dependent manner during catalysis. Although this observation has been reported and characterized for several different systems 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 mechanisms. 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 ththe 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.
227-230 (2015) pdf version
Counter Argument Paper Enhanced Diffusion of Enzymes that Catalyze Exothermic Reactions
author = Ramin Golestanian abstract
Enzymes have been recently found to exhibit enhanced diffusion due to their catalytic activities. A recent experiment [C. Riedel et al.
, Nature (London) 517
, 227 (2015)] has found evidence that suggests this phenomenon might be controlled by the degree of exothermicity of the catalytic reaction involved. Four mechanisms that can lead to this effect, namely, self-thermophoresis, boost in kinetic energy, stochastic swimming, and collective heating are critically discussed, and it is shown that only the last two can be strong enough to account for the observations. The resulting quantitative description is used to examine the biological significance of the effect.
article 108102 (2015) pdf version
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