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Updated: May 14, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
Role of diffusion in the kinetics of reversible enzyme-catalyzed reactions
Attila Szabo1, Huan-Xiang Zhou
1Laboratory of Chemical Physics, National Institute of Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
Abstract:
The accurate expression for the steady-state velocity of an irreversible enzyme-catalyzed reaction obtained by Shin and co-workers is generalized to allow for the rebinding of the product. The amplitude of the power-law (t(-1/2)) relaxation of the free- and bound-enzyme concentrations to steady-state values is expressed in terms of the steady-state velocity and the intrinsic (chemical) rate constants. This result is conjectured to be exact, even though our expression for the steady-state velocity in terms of microscopic parameters is only approximate.
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