When a biochemical reaction is carried out in the laboratory, outside the human body in the absence of the enzyme, then the rate of reaction obtained is 10^–6 times, the activation energy of reaction in the presence of enzyme is:

Different from E_a obtained in the laboratory

The correct answer is option 3. Different from \(E_a\) obtained in the laboratory.

The Role of Enzymes in Biochemical Reactions

Enzymes as Catalysts:

Enzymes are biological catalysts that speed up biochemical reactions. They achieve this by lowering the activation energy \((E_a)\) needed for the reaction to proceed.

Activation Energy:

Activation energy is the minimum energy required for reactants to undergo a chemical reaction. In the presence of an enzyme, the activation energy is reduced, allowing the reaction to proceed faster.

The Given Information

Reaction Rate Comparison:

The rate of the reaction in the absence of the enzyme is \(10^{-6}\) times the rate of the reaction with the enzyme.This means the reaction is significantly slower without the enzyme.

Applying the Arrhenius Equation

The Arrhenius equation relates the rate constant \(k\) to the activation energy \(E_a\):

\(k = A e^{-E_a / (RT)} \)

\(k\): Rate constant of the reaction

\(A\): Pre-exponential factor (frequency of collisions with proper orientation)

\(E_a\): Activation energy

\(R\): Universal gas constant

\(T\): Temperature in Kelvin

Analyzing the Rate Difference

If the reaction rate is \(10^6\) times faster with the enzyme, it implies that the activation energy is significantly lowered by the enzyme. A lower activation energy \(E_a\) leads to a much higher rate constant \(k\).

Interpreting the Options

6/RT: This option seems to suggest a specific numerical value, but without context or derivation, it's unclear how it relates to the provided information.

P is required: This option is vague and lacks clarity.

Different from Ea obtained in the laboratory: This option accurately reflects the situation. The activation energy in the presence of the enzyme is different (specifically, much lower) than the activation energy measured without the enzyme.

Can’t say anything: This option is not accurate because we do have enough information to conclude that the activation energy is significantly different when the enzyme is present.

Conclusion

The enzyme's presence drastically lowers the activation energy, leading to a much faster reaction rate. Therefore, the correct statement is: Different from \(E_a\) obtained in the laboratory.

This indicates that the activation energy in the presence of the enzyme is different from (specifically, much lower than) the activation energy without the enzyme.