Why are Hydrophobic Interactions Relevant in Catalysis?
Hydrophobic interactions play a crucial role in the stability and activity of catalysts, especially in biological and heterogeneous catalysis. For instance, in enzyme catalysis, the hydrophobic amino acid residues often form the active site where the substrate binds. This hydrophobic environment can enhance the binding affinity of nonpolar substrates, improving the catalytic efficiency. Similarly, in heterogeneous catalysis, the hydrophobicity of the catalyst's surface can impact adsorption-desorption equilibria, affecting the overall reaction rate.
