Enzymes catalyze reactions with high rates and selectivities through the sophisticated use of cooperative interactions between neighboring functional groups within an active site. For example, the “catalytic triad” in proteases is capable of accelerating the cleavage of amides by 1011 through neighboring interactions between carboxylic acid, imidazole, and alcohol sites. Guided by these principles, heterogeneous catalysts having two different types of functional groups have been prepared, and the cooperative behavior have been demonstrated with catalytic reactions in the liquid phase. Cooperative interactions between thiols and sulfonic acids and between incompatible acid and base groups are achievable with rates and selectivities that are superior to homogeneous systems, especially for the latter case wherein there is no reactivity.