Enzyme Catalysis
Enzymes accelerate reactions by primarily:
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About This Question
- Subject
- chemistry
- Chapter
- biomolecules
- Topic
- enzyme catalysis
- Difficulty
- Medium
- Year
- 2025
Solution
Correct Answer:
Lowering activation energy via transition state stabilization
- Catalysis Principle: A catalyst speeds up a reaction without being consumed by providing an alternative reaction pathway.
- Activation Energy (Ea): The energy barrier that reactants must overcome to reach the Transition State.
- Mechanism: Enzymes bind substrates in an 'active site' tailored to stabilize the Transition State (ES complex).
- Result: By reducing the energy required to reach this state, the activation energy is lowered, allowing more molecules to react at a given temperature.
- Caution: Enzymes do NOT change the equilibrium constant (no change in ΔG∘).
This medium difficulty chemistry question is from the chapter biomolecules, covering the topic of enzyme catalysis. It appeared in the 2025 exam.
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