Volume 119, Number 4, August 2017
|Number of page(s)||7|
|Published online||03 November 2017|
Diffusion of an enzyme: The role of fluctuation-induced hydrodynamic coupling
1 Rudolf Peierls Centre for Theoretical Physics, University of Oxford - Oxford OX1 3NP, UK
2 Department of Chemistry, The Pennsylvania State University - University Park, PA 16802, USA
Received: 25 August 2017
Accepted: 11 October 2017
The effect of conformational fluctuations of modular macromolecules, such as enzymes, on their diffusion properties is addressed using a simple generic model of an asymmetric dumbbell made of two hydrodynamically coupled subunits. It is shown that equilibrium fluctuations can lead to an interplay between the internal and the external degrees of freedom and give rise to negative contributions to the overall diffusion coefficient. Considering that this model enzyme explores a mechanochemical cycle, we show how substrate binding and unbinding affects its internal fluctuations, and how this can result in an enhancement of the overall diffusion coefficient of the molecule. These theoretical predictions are successfully confronted with recent measurements of enzyme diffusion in dilute conditions using fluorescence correlation spectroscopy.
PACS: 05.40.-a – Fluctuation phenomena, random processes, noise, and Brownian motion / 82.39.Fk – Enzyme kinetics / 47.63.mf – Low-Reynolds-number motions
© EPLA, 2017
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