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The effect of conformational fluctuations of modular macromolecules, such asenzymes, on their diffusion properties is addressed using a simple genericmodel of an asymmetric dumbbell made of two hydrodynamically coupled subunits.It is shown that equilibrium fluctuations can lead to an interplay between theinternal and the external degrees of freedom and give rise to negativecontributions to the overall diffusion coefficient. Considering that this modelenzyme explores a mechanochemical cycle, we show how substrate binding andunbinding affects its internal fluctuations, and how this can result in anenhancement of the overall diffusion coefficient of the molecule. Thesetheoretical predictions are successfully confronted with recent measurements ofenzyme diffusion in dilute conditions using fluorescence correlationspectroscopy.

Diffusion of an Enzyme: the Role of Fluctuation-Induced Hydrodynamic Coupling