Question

The efficiency of an enzyme to catalyse a reaction is due to its capacity to (a) reduce the activation energy of the reaction (b) form strong enzyme substrate complex (c) decrease the bond energy of all substrate molecules (d) increase the free energy of the catalyst substrate reaction (e) alter the substrate geometry to fit into the shape of the enzyme molecule.

Short answer

(a) reduce the activation energy of the reaction.

Step-by-step solution

Understanding Enzyme Catalysis

Enzymes increase the rate of a reaction by lowering the activation energy, which is the energy barrier for the reaction to occur. This is a fundamental property of enzymes and is related to option (a).

Analyzing the Given Options

Let's analyze each option: (a) Enzymes lower the activation energy, (b) Strong enzyme-substrate complexes can be part of the process, but it's the ability to lower activation energy that defines enzyme efficiency, (c) Decreasing bond energy is not correct as it refers to the entire substrate, (d) Enzymes do not increase free energy; reactions may become more spontaneous, but free energy is not increased, (e) Enzymes might alter substrate geometry (induced fit), but the fundamental role in catalysis is reducing activation energy.

Comparing Options with Enzyme Function

By comparing the main function of enzymes in catalyzing reactions (lowering activation energy) against the provided options, we identify that option (a) matches the core role of an enzyme in catalysis.

Key concepts

Activation Energy

Activation energy is a key concept when discussing enzyme catalysis. In simple terms, activation energy is the minimum energy required for a chemical reaction to occur. Imagine it like a hill that a reaction must climb; the higher the hill, the more energy is needed to get over it. Enzymes play a crucial role in lowering this activation energy. By reducing the height of the hill, enzymes allow reactions to happen more quickly and efficiently without needing as much energy.

This reduction in activation energy is vital because it essentially speeds up the rate of the reaction. Enzymes achieve this by providing an alternative reaction pathway with a lower energy requirement. This is why enzymes are known as catalysts—they make reactions "easier" by reducing the effort needed to start them. Understanding this concept helps explain why enzymes are so efficient and fundamentally important in biological systems.

Enzyme-Substrate Complex

An enzyme-substrate complex forms when an enzyme binds to its specific substrate, which is the molecule upon which the enzyme acts. This complex is a temporary state that is crucial for the catalytic process. When the substrate binds to the enzyme, they form a specific structure that allows the enzyme to perform its catalytic function.

**Formation and Function**

• Firstly, the substrate binds to the enzyme at a specific area called the active site.
• The active site is uniquely shaped to fit only specific substrates, which grants enzymes their specificity.
• The binding of the substrate forms the enzyme-substrate complex, facilitating a series of interactions that lead to the chemical reaction.
• Once the reaction is complete, the product is released, and the enzyme is free to interact with another substrate molecule.

This temporary union ensures that enzymes can efficiently catalyze reactions repeatedly without being consumed in the process.

Induced Fit Model

The induced fit model offers an excellent explanation of how enzyme-substrate interaction occurs beyond the simple "lock and key" analogy. While the active site of the enzyme is shaped to fit the substrate, enzymes are flexible and can adjust in shape to better fit the substrate.

**Understanding Induced Fit**

• Initially, the substrate binds to the enzyme weakly.
• This binding prompts a conformational change in the enzyme's structure, allowing a tighter fit around the substrate.
• The repositioning enhances the enzyme's ability to catalyze the conversion of the substrate into products.
• The induced fit model highlights the dynamic nature of enzymes, showing that binding can trigger structural adaptations that optimize catalysis.

Hence, the induced fit model emphasizes the adaptability of enzymes, showcasing their capability to maximize reaction efficiency through structural adjustments during substrate interaction.