The rate enhancements obtained by enzymes often require greater than 20 kcal/mol of stabilization that is specific to the transition state. Inspection of active sites suggests that enzymes often use multiple interactions with substrate groups undergoing charge rearrangement to help provide this preferential stabilization. We have analyzed the deprotonation, in DMSO, of benzoic acids with one or two hydrogen bond donating substituents ortho to the carboxylic acid. This provides a model for the ability of multiple hydrogen bonds to facilitate reactions at enzymatic active sites. The simplicity of this model has allowed the energetic contributions of the hydrogen bonds to be isolated and assessed quantitatively. It was found that one and two hydrogen bonds from the hydroxyl group(s) ortho to the carboxyl group provide specific stabilization of the carboxylate relative to the carboxylic acid by 7.9 and 14.4 kcal/mol, respectively. The energetic contribution of the two hydrogen bonds is nearly additive. This provides a quantitative demonstration of the basic principle that the energy of multiple interactions, each of moderate strength, can be combined to make a significant contribution to enzymatic catalysis.