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Ch. 8 - Energy and Enzymes: An Introduction to Metabolism
Chapter 8, Problem 4

What factors determine whether a chemical reaction is spontaneous or not?

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1. The spontaneity of a chemical reaction is determined by two main factors: the change in enthalpy (ΔH) and the change in entropy (ΔS).
2. The change in enthalpy (ΔH) refers to the total energy change of the system. If the reaction releases energy (exothermic), ΔH is negative and the reaction is more likely to be spontaneous. If the reaction absorbs energy (endothermic), ΔH is positive and the reaction is less likely to be spontaneous.
3. The change in entropy (ΔS) refers to the change in disorder or randomness. If the reaction results in an increase in disorder (positive ΔS), it is more likely to be spontaneous. If the reaction results in a decrease in disorder (negative ΔS), it is less likely to be spontaneous.
4. However, both these factors are considered together in the Gibbs free energy equation: ΔG = ΔH - TΔS. If ΔG is negative, the reaction is spontaneous. If ΔG is positive, the reaction is non-spontaneous.
5. Temperature (T) also plays a role in determining the spontaneity of a reaction. At high temperatures, the entropy term (TΔS) can dominate, making reactions with positive ΔS but positive ΔH spontaneous.

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Key Concepts

Here are the essential concepts you must grasp in order to answer the question correctly.

Gibbs Free Energy

Gibbs Free Energy (G) is a thermodynamic potential that helps predict the spontaneity of a chemical reaction. A reaction is spontaneous if the change in Gibbs Free Energy (ΔG) is negative, indicating that the process can occur without external energy input. The relationship is given by the equation ΔG = ΔH - TΔS, where ΔH is the change in enthalpy, T is the temperature in Kelvin, and ΔS is the change in entropy.
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Enthalpy and Entropy

Enthalpy (H) is a measure of the total heat content of a system, while entropy (S) quantifies the degree of disorder or randomness. A spontaneous reaction typically involves a decrease in enthalpy (exothermic) or an increase in entropy. Understanding how these two factors interact is crucial for determining the overall spontaneity of a reaction, as they contribute to the Gibbs Free Energy change.
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Temperature's Role

Temperature plays a significant role in determining the spontaneity of a reaction, as it affects both enthalpy and entropy. The term TΔS in the Gibbs Free Energy equation shows that at higher temperatures, the impact of entropy becomes more pronounced. This means that reactions with a positive ΔS can become spontaneous at elevated temperatures, even if they are endothermic (positive ΔH).
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Related Practice
Textbook Question

Which of the following correctly describe an exergonic reaction? Select True or False for each statement. T/F The products have lower Gibbs free energy than the reactants. T/F Activation energy is required for the reaction to proceed. T/F The products always have lower entropy than the reactants. T/F The reaction always occurs quickly.

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Textbook Question

What is a transition state? a. the shape adopted by an enzyme that has an inhibitory molecule bound at its active site b. the amount of kinetic energy required for a reaction to proceed c. the intermediate complex formed as covalent bonds in the reactants are being broken and re-formed during a reaction d. the enzyme shape after binding an allosteric regulatory molecule

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Textbook Question

How does pH affect enzyme-catalyzed reactions? a. Protons serve as substrates for most reactions. b. Energy stored in protons is used to drive endergonic reactions. c. Proton concentration increases the kinetic energy of the reactants, enabling them to reach their transition state. d. The concentration of protons affects an enzyme's folded structure and reactivity.

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Textbook Question

Which of the following correctly describe an active site? Select True or False for each statement. T/F It is the location in an enzyme where substrates bind. T/F It is the place where a molecule or ion binds to an inactive enzyme to induce a shape change to make it active. T/F It is the portion of an enzyme where chaperones bind to help enzymes fold. T/F It is the site on an enzyme where catalysis occurs.

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Textbook Question

Explain the lock-and-key model of enzyme activity. What is incorrect about this model?

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Textbook Question

If you were to expose glucose to oxygen on your lab bench, why would you not expect to see it burn as described by the reaction in Figure 8.6? a. The reaction is endergonic and requires an input of energy. b.The reaction is not spontaneous unless an enzyme is added. c. The sugar must first be phosphorylated to increase its potential energy. d. Activation energy is required for the sugar and oxygen to reach their transition state.

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