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Department of Chemistry, James Franck Institute, Institute for Biophysical Dynamics, and Committee on Immunology, The University of Chicago, Chicago, Illinois
Correspondence: Address reprint requests to A. R. Dinner, Tel: 773-702-2330; Fax: 773-834-5250; E-mail: dinner{at}uchicago.edu.
We explore the means by which immobilization of a substrate on a surface can increase the rate of a diffusion-controlled enzymatic reaction. A quasichemical approach is developed and compared with Brownian dynamics simulations. We use these methods to show that restricting only the orientation of the enzyme by long-range interactions with the surface is sufficient for enhancing catalysis.
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