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What general effects would you expect the following changes to have on the rate of an enzyme-catalyzed reaction for an enzyme that has its maximum activity at body temperature (about \(\left.37^{\circ} \mathrm{C} / 310.15 \mathrm{~K}\right)\) ? (a) Lowering the reaction temperature from \(313 \mathrm{~K}\left(40{ }^{\circ} \mathrm{C}\right)\) to \(283 \mathrm{~K}\left(10^{\circ} \mathrm{C}\right)\) (b) Adding a drop of a dilute \(\mathrm{HgCl}_{2}\) solution (c) Adding an oxidizing agent, such as hydrogen peroxide

Short Answer

Expert verified
(a) Decrease in reaction rate; (b) Decrease or inhibit reaction rate; (c) Decrease or inhibit reaction rate.

Step by step solution

01

Analyzing Temperature Changes

Enzyme activity is affected by temperature changes. Generally, enzyme-catalyzed reactions increase in rate as temperature increases, up to a point. If the temperature lowers from above the optimum (40°C) to significantly below it (10°C), the reaction rate will decrease. This is because the molecules have less kinetic energy at lower temperatures, resulting in fewer successful collisions and consequently, a slower reaction rate.
02

Evaluating the Effect of Mercuric Chloride (HgCl₂) Solution

Mercuric chloride ( HgCl₂) is a heavy metal ion that can inhibit enzyme activity by binding to amino acids, particularly cysteine residues, in enzymes. This binding can lead to conformational changes or block active sites, thus reducing the enzyme's activity or completely denaturing the enzyme. Therefore, adding a drop of a dilute HgCl₂ solution is likely to decrease the reaction rate.
03

Understanding the Effect of an Oxidizing Agent like Hydrogen Peroxide

Oxidizing agents such as hydrogen peroxide can cause the oxidation of side chains or critical groups in the enzyme, potentially leading to changes in enzyme structure or the denaturation of the enzyme. This can significantly affect the enzyme's ability to catalyze reactions, often resulting in a decreased reaction rate or inhibition of the enzyme.

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Key Concepts

These are the key concepts you need to understand to accurately answer the question.

Temperature Effect on Enzymes
Temperature plays a significant role in enzyme activity. Enzymes, being proteins, have an optimal temperature at which they function most efficiently. For human enzymes, this temperature is typically around 37°C (310.15 K). When the temperature is reduced, the kinetic energy of molecules involved in the reaction also decreases.
  • This results in fewer collisions between enzyme and substrate molecules, thereby slowing down the rate of reaction.
  • As a result, lowering the temperature drastically, like from 40°C to 10°C, significantly reduces enzyme activity because the enzymes are not operating under their optimal conditions.
Enzymatic reactions occur more slowly at lower temperatures, illustrating why organisms often function within a narrow temperature range.
Enzyme Inhibitors
Enzyme inhibitors are substances that can reduce or completely stop enzyme activity. There are different types of inhibitors, but heavy metals like mercuric chloride (HgCl₂) are significant due to their capacity to bind with enzymes.
  • Mercuric chloride can interact with enzymes by binding to sulfhydryl groups found on the amino acid cysteine in enzymes.
  • Such binding can alter the enzyme's shape, obstruct its active site, diminish its activity, or denature it entirely.
Therefore, introducing a small amount of mercuric chloride into a reaction containing a sensitive enzyme typically decreases the reaction rate, illustrating how potent inhibitors can affect enzymatic processes.
Oxidizing Agents and Enzyme Activity
Oxidizing agents, such as hydrogen peroxide, can significantly impact enzyme activity. These agents can alter the structure and function of enzymes through oxidation.
  • Oxidizing agents might modify essential amino acids in the enzyme, disrupting its normal functionality.
  • The change in structure can lead to enzyme denaturation, rendering the enzyme unable to facilitate its intended chemical reaction.
By causing such structural changes, oxidizing agents can drastically decrease enzyme activity, highlighting the importance of maintaining specific conditions in biochemical reactions to ensure efficient enzymatic activity.

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Most popular questions from this chapter

Amino acid side chains in the active sites of enzymes can act as acids or bases during catalysis. List the amino acid side chains that can accept \(\mathrm{H}^{+}\) and those that can donate \(\mathrm{H}^{+}\) during enzyme- catalyzed reactions.

EcoRI, an enzyme that hydrolyzes DNA strands, requires \(\mathrm{Mg}^{2+}\) as a cofactor for activity. EDTA chelates divalent metal ions in solution. In the graphs shown here, the arrow indicates the point at which EDTA is added to a reaction mediated by EcoRI. Which graph represents the activity curve you would expect to see? (Activity is shown as total product from the reaction as time increases.)

(a) \(\mathrm{L}\) -Threonine is converted to \(\mathrm{L}\) -isoleucine in a linear pathway involving five separate enzymes. Which of the enzymes in the following pathway is most likely inhibited by the product of the pathway, \(\mathrm{L}\) -isoleucine? L-threonine \(\stackrel{\mathrm{E} 1}{\longrightarrow} \mathrm{A} \stackrel{\mathrm{E} 2}{\longrightarrow} \mathrm{B} \stackrel{\mathrm{E} 3}{\longrightarrow} \mathrm{C} \stackrel{\mathrm{E} 4}{\longrightarrow} \mathrm{D} \stackrel{\mathrm{E} 5}{\longrightarrow} \mathrm{L}\) -isoleucine (b) If product A inhibited the first enzyme in the pathway (E1), could this be called feedback control? Explain.

Activation of a zymogen is by covalent modification. How might phosphorylation or dephosphorylation (also covalent modification) modify an enzyme to make it more active (or more inactive)?

Why is the induced-fit model a more likely model than the lock-and-key model?

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