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Multiple Choice
If an enzyme increases the rate of the hydrolysis reaction by a factor of 1 million, how much lower must the activation energy barrier be when sucrose is involved?
A
Approximately 1 kcal/mol lower
B
Approximately 20 kcal/mol lower
C
Approximately 10 kcal/mol lower
D
Approximately 5.7 kcal/mol lower
Verified step by step guidance
1
Understand the relationship between the rate of a reaction and the activation energy. The rate of a reaction is exponentially related to the activation energy through the Arrhenius equation: \( k = A e^{-\frac{E_a}{RT}} \), where \( k \) is the rate constant, \( A \) is the pre-exponential factor, \( E_a \) is the activation energy, \( R \) is the gas constant, and \( T \) is the temperature.
Recognize that the enzyme increases the rate of the reaction by a factor of 1 million. This means the rate constant \( k \) with the enzyme is 1 million times greater than the rate constant \( k_0 \) without the enzyme.
Set up the equation relating the rate constants with and without the enzyme: \( \frac{k}{k_0} = e^{-\frac{E_a - E_{a0}}{RT}} = 1,000,000 \), where \( E_a \) is the activation energy with the enzyme and \( E_{a0} \) is the activation energy without the enzyme.
Take the natural logarithm of both sides to solve for the change in activation energy: \( \ln(1,000,000) = -\frac{E_a - E_{a0}}{RT} \).
Rearrange the equation to find the difference in activation energy: \( E_{a0} - E_a = RT \ln(1,000,000) \). Use the value of \( R \) (approximately 1.987 cal/mol·K) and assume a typical temperature (e.g., 298 K) to calculate the approximate change in activation energy.