Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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Role of Diffusion in the Kinetics of Reversible Enzyme-catalyzed Reactions

  • Szabo, Attila (Laboratory of Chemical Physics, National Institute of Digestive and Kidney Diseases, National Institutes of Health) ;
  • Zhou, Huan-Xiang (Department of Physics and Institute of Molecular Biophysics, Florida State University)
  • Received : 2011.09.16
  • Accepted : 2012.01.06
  • Published : 2012.03.20
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Abstract

The accurate expression for the steady-state velocity of an irreversible enzyme-catalyzed reaction obtained by Shin and co-workers (J. Chem. Phys. 2001, 115, 1455) 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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References

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