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Question
a researcher proposes a model of an enzyme - catalyzed reaction in which a reactant is converted to a product. the model is based on the idea that the reactant passes through a transition state within the enzyme - substrate complex before the reactant is converted to the product. which of the following statements best helps explain how the enzyme speeds up the reaction? a the enzymes active site binds to and stabilizes the reactant, which decreases the free - energy change of the reaction. b the enzymes active site binds to and stabilizes the transition state, which decreases the activation energy of the reaction. c the enzymes active site binds to and stabilizes the product, which increases the amount of energy released by the reaction. d the enzymes active site binds to and stabilizes both the reactant and the product at the same time, which increases the reactions equilibrium constant.
Enzymes speed up reactions by lowering activation energy ($E_a$), the energy needed to reach the transition state. Stabilizing the transition state reduces $E_a$, allowing more reactants to overcome this barrier and react faster. Option A is wrong because enzymes don’t change the free-energy change ($\Delta G$) of the reaction. Option C is incorrect as stabilizing products doesn’t increase energy release (which is fixed by $\Delta G$). Option D is false because enzymes don’t alter the equilibrium constant; they only speed up reaching equilibrium. Thus, B is the correct explanation.
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B. The enzyme’s active site binds to and stabilizes the transition state, which decreases the activation energy of the reaction.