Oct 24, 2018

A Thermodynamic Limit on the Role of Self-Propulsion in Enhanced Enzyme Diffusion

BioRxiv : the Preprint Server for Biology
Mudong Feng, Michael K Gilson

Abstract

A number of enzymes reportedly exhibit enhanced diffusion in the presence of their substrates, with a Michaelis-Menten-like concentration dependence. Although no definite explanation of this phenomenon has emerged, a physical picture of enzyme self-propulsion using energy from the catalyzed reaction has been widely considered. Here, we present a kinematic and thermodynamic analysis of enzyme self-propulsion that is independent of any specific propulsion mechanism. Using this theory, along with biophysical data compiled for all enzymes so far shown to undergo enhanced diffusion, we show that the propulsion speed required to generate experimental levels of enhanced diffusion exceeds the speeds of well-known active biomolecules, such as myosin, by several orders of magnitude. Furthermore, the minimum power dissipation required to account for enzyme enhanced diffusion by self-propulsion markedly exceeds the chemical power available from enzyme-catalyzed reactions. Alternative explanations for the observation of enhanced enzyme diffusion therefore merit stronger consideration.

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Mentioned in this Paper

Enzymes, antithrombotic
Clinical Enzyme Tests (Procedure)
Biophysics
Kinematics
Enzymes for Treatment of Wounds and Ulcers
Myosin ATPase
Analysis
Enzymes, hematological
Enzymology
Enzymes for Disorders of The Musculo-Skeletal System

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