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 |
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| Authors: | Roberts J D Kanamori K |
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| Affiliation: | Gates and Crellin Laboratories of Chemistry, California Institute of Technology, Pasadena, California 91125. |
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| Abstract: | 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°C have been measured by NMR spectroscopy. |
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