Roberts, John D. and Kanamori, Keiko (1980) Benzoate catalysis in the hydrolysis of endo-5-[4'(5')imidazolyl]-bicyclo[2.2.1]hept-endo-2-yl trans-cinnamate: Implications for the charge-transfer mechanism of catalysis by serine proteases. Proceedings of the National Academy of Sciences of the United States of America, 77 (6). pp. 3095-3097. ISSN 0027-8424 http://resolver.caltech.edu/CaltechAUTHORS:ROBpnas80
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The acceleration, by a factor of 2500, of the hydrolysis of endo-5-[4'(5')imidazolyl]bicyclo[2.2.1]hept-endo-2-yl trans-cinnamate by 0.5 M sodium benzoate in 42 mol% dioxane in water can be explained without resort to operation of a "charge-relay" mechanism similar to that often postulated to account for the enzymatic activity of serine proteases. The degree of ionization of 4-methylimidazole and of sodium benzoate in 42 mol% dioxane in water at 60 degrees C have been measured by NMR spectroscopy.
|Additional Information:||© 1980 by the National Academy of Sciences. Contributed by John D. Roberts, February 19, 1980. We thank Profs. J.H. Richards and W. W. Bachovchin for many helpful suggestions. This is contribution no. 6173 from the Gates and Crellin Laboratories of Chemistry. These studies were supported by U.S. Public Health Service Grant GM-11072 from the Division of General Medical Sciences and by the National Science Foundation.|
|Subject Keywords:||13C and 15N NMR spectroscopy; ester hydrolysis; base catalysis; medium effects on reaction rates; enzyme mechanisms|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Tony Diaz|
|Deposited On:||15 Apr 2008|
|Last Modified:||26 Dec 2012 09:57|
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