Final answer:
The statement is true; enzymes increase reaction rates by binding to substrates, inducing conformational changes to stabilize the transition state and lower the activation energy, which makes the chemical reaction proceed faster.
Step-by-step explanation:
The statement that enzymes increase the rates of chemical reactions by binding to transition states of the reaction and thereby making them more likely to occur is true. Enzymes are biological catalysts that accelerate chemical reactions by lowering their activation energy.
The enzyme provides a unique chemical environment at its active site, where substrates—the reactants of a biochemical reaction—are bound. This environment includes optimal orientation of substrates and stabilization of the transition state, which refers to the high-energy, transient state during the conversion of substrates into products.
Enzymes work via an induced-fit model where both enzyme and substrate undergo conformational changes to achieve ideal binding. This contorts the substrate into its transition state, effectively lowering the energy barrier for the reaction and increasing its rate.
Thus, enzymes facilitate chemical reactions by securing substrates in the correct orientation, distorting substrate bonds to make them easier to break, and even forming transient covalent bonds with the substrates, which are all ways to stabilize the transition state and speed up the reaction.
Once the reaction is complete, the product is released, and the enzyme can return to catalyze other reactions without being consumed in the process.