Enzyme Catalysis
Mediumchemistry
Enzymes accelerate reactions by primarily:
Select the correct option:
Solution
Incorrect! 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 (Eaā): 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 ĪGā).
š Solution Hidden from View
Submit your answer to unlock the detailed step-by-step solution.
More enzyme catalysis Practice Questions
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 (Eaā): 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 ĪGā).
This medium difficulty chemistry question is from the chapter biomolecules, covering the topic of enzyme catalysis. It appeared in the 2025 exam.
Looking for more practice? Explore all chemistry questions or browse biomolecules questions on RankGuru.