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Most reactions, including enzyme-catalyzed reactions, proceed faster at higher temperatures. However, for a given enzyme, the rate drops off abruptly at a certain temperature. Account for this behavior.

Short Answer

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Enzymes increase reaction rates with higher temperatures until denaturation occurs, reducing their activity.

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01

Understand Enzyme Activity and Temperature

Enzymes are biological catalysts that speed up chemical reactions in cells. As temperature increases, the kinetic energy of molecules also increases, leading to more frequent collisions between enzymes and substrates, thus increasing the reaction rate.
02

Identify the Optimal Temperature

For each enzyme, there is an optimal temperature at which the enzyme activity is at its peak. This is the temperature at which the enzyme structure is most conducive to catalyzing the reaction efficiently.
03

Explain Denaturation of Enzymes

Beyond the optimal temperature, the enzyme may begin to denature, losing its specific three-dimensional structure. Denaturation disrupts the active site, where the substrate binds to the enzyme, leading to a decrease in enzyme activity.
04

Connect Temperature Increase and Rate Decrease

As the temperature continues to rise past the optimal point, denaturation becomes more significant and abrupt, causing the enzyme to become inactive. The decrease in the number of functioning enzyme molecules leads to a rapid decline in the reaction rate.

Key Concepts

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

Enzyme Denaturation
Enzymes are delicate molecules that catalyze chemical reactions in cells efficiently. However, they can be quite sensitive to changes in environmental conditions, such as temperature. At elevated temperatures, enzymes can undergo a process called denaturation. This means that their intricate three-dimensional structures—essential for their function—begin to unravel and change. When an enzyme denatures, its active site, where the chemical reactions occur, gets distorted.
  • Denaturation is often irreversible.
  • The enzyme's ability to catalyze reactions diminishes or is completely lost.
Importantly, denaturation doesn't break the peptide bonds within the enzyme but rather disrupts the bonds that maintain its shape and function. Once an enzyme denatures, even reducing the temperature back to optimal levels won't restore its original structure and activity.
Optimal Temperature
Every enzyme has a specific optimal temperature range where it catalyzes reactions most efficiently. When enzymes function within this range, they adopt the most favorable conformation to facilitate reactions. The optimal temperature aligns with the environment the enzyme naturally operates in. For example:
  • Human enzymes typically have an optimal temperature near 37°C, which is body temperature.
  • Thermophilic bacteria, which live in hot springs, have enzymes optimal at much higher temperatures.
When an enzyme is at its optimal temperature, the increased kinetic energy of molecules enhances collisions between enzyme and substrate. This perfect balance leads to a peak in enzyme activity.
Reaction Rate
The reaction rate, in the context of enzyme activity, is how fast a substrate is converted into a product. As temperature increases, so does the reaction rate—up to a point. This increase in rate occurs because higher temperatures raise molecular motion, increasing the chances of enzyme and substrate interactions. But there’s a catch:
  • Beyond the optimal temperature, the reaction rate declines due to enzyme denaturation.
  • The abrupt slowdown is often because enzymes, losing their shape from heat, no longer bind to substrates effectively.
Therefore, while higher temperatures initially boost the reaction rate, once the temperature exceeds the optimal level, the efficiency declines sharply due to damaged enzyme structures.

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Most popular questions from this chapter

What is the half-life of a compound if 75 percent of a given sample of the compound decomposes in \(60 \mathrm{~min}\) ? Assume first-order kinetics.

The rate law for the following reaction: $$ \mathrm{CO}(g)+\mathrm{NO}_{2}(g) \longrightarrow \mathrm{CO}_{2}(g)+\mathrm{NO}(g) $$ is rate \(=k\left[\mathrm{NO}_{2}\right]^{2}\). Suggest a plausible mechanism for the reaction, given that the unstable species \(\mathrm{NO}_{3}\) is an intermediate.

When \(6 \mathrm{~g}\) of granulated \(\mathrm{Zn}\) is added to a solution of \(2 \mathrm{M}\) \(\mathrm{HCl}\) in a beaker at room temperature, hydrogen gas is generated. For each of the following changes (at constant volume of the acid) state whether the rate of hydrogen gas evolution will be increased, decreased, or unchanged: (a) \(6 \mathrm{~g}\) of powdered \(\mathrm{Zn}\) is used, (b) \(4 \mathrm{~g}\) of granulated \(\mathrm{Zn}\) is used, (c) \(2 M\) acetic acid is used instead of \(2 M \mathrm{HCl}\), (d) temperature is raised to \(40^{\circ} \mathrm{C}\).

(a) Consider two reactions, \(\mathrm{A}\) and \(\mathrm{B}\). If the rate constant for reaction B increases by a larger factor than that of reaction A when the temperature is increased from \(T_{1}\) to \(T_{2},\) what can you conclude about the relative values of the activation energies of the two reactions? (b) If a bimolecular reaction occurs every time an \(\mathrm{A}\) and a \(\mathrm{B}\) molecule collide, what can you say about the orientation factor and activation energy of the reaction?

For the reaction: $$ \mathrm{NO}(g)+\mathrm{O}_{3}(g) \longrightarrow \mathrm{NO}_{2}(g)+\mathrm{O}_{2}(g) $$ the frequency factor \(A\) is \(8.7 \times 10^{12} \mathrm{~s}^{-1}\) and the activation energy is \(63 \mathrm{~kJ} / \mathrm{mol}\). What is the rate constant for the reaction at \(75^{\circ} \mathrm{C} ?\)

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