Final answer:
The transition state oxyanion in chymotrypsin catalysis is stabilized by specific amino acid residues in the enzyme's active site, which can form hydrogen bonds and perform acid-base catalysis. The stability of the product is also enhanced by the stabilization of the C=C bond through conjugation with a C=O group.
Step-by-step explanation:
The transition state oxyanion that forms during chymotrypsin catalysis is stabilized by several factors within the enzyme's active site. Experimental data shows that key amino acid residues, often His, Cys, Asp, Arg, and Glu, are critical for catalysis. These amino acids can engage in hydrogen bonding and acid-base catalysis, which are crucial for enzymatic reactions. Additionally, the stabilization of the C=C bond by a conjugated C=O group can make the product more stable, effectively lowering the activation energy for the reaction.
Dynamic changes undergone by both enzyme and substrate also contribute to the stabilization of the transition state. The structural rigidity imparted by the protein scaffold, and possible involvement of co-factors like Mg2+ ions, further ensure the stabilization of high-energy intermediates. This allows for more efficient turnover of substrate into product. For instance, interactions with coenzymes such as FAD and FADH₂ could also be relevant in other enzymatic contexts.