Biological Science (7th Edition)
7th Edition
ISBN: 9780134678320
Author: Scott Freeman, Kim Quillin, Lizabeth Allison, Michael Black, Greg Podgorski, Emily Taylor, Jeff Carmichael
Publisher: PEARSON
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Textbook Question
Chapter 8, Problem 8TYU
Using what you have learned about changes in Gibbs free energy, would you predict the AG value of catabolic reactions to be positive or negative? What about anabolic reactions? Justify your answers using the terms “enthalpy” and “entropy.”
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Students have asked these similar questions
Which of the following statements are true for BOTH the "transition state" and an
"intermediate" of reaction? (This is a multi-select question, select all that apply.).
Both are only observed in enzyme-catalyzed reactions.
Both can be converted to product(s) or might decompose back to the reactant(s).
Neither are part of the "net equation" for the reaction.
Both contain covalent bonds are in the process of breaking and/or forming.
Both are part of every chemical reaction. (i.e. the mechanisms of all chemical
reactions, whether enzyme catalyzed or not, will have involve both a transition
state and an intermediate).
A particular reaction has a ΔG‡ of 37.0 kJ mol-1. In the presence of an enzyme, the same reaction has a ΔG‡ of 5.70 kJ mol-1. Calculate the value of ΔΔG‡ in kJ mol-1.
Determine the direction that each of the reactions will progress.
Assume that the reactants and products are present in equimolar amounts. The standard free energy of hydrolysis of ATP is
- 30.5 kJ/mol.
fructose + ATP
fructose 6-phosphate + ADP
The standard free energy of hydrolysis for fructose 6-phosphate is -15.9 kJ/mol.
3-phosphoglycerate + ATP
1,3-bisphosphoglycerate + ADP
The standard free energy of hydrolysis for 1,3-bisphosphoglycerate is -49.3 kJ/mol.
creatine + ATP
creatine phosphate + ADP
The standard free energy of hydrolysis for creatine phosphate is -43.0 kJ/mol.
Chapter 8 Solutions
Biological Science (7th Edition)
Ch. 8 - 2. What is a transition state?
a. the shape...Ch. 8 - 3. How does pH affect enzyme-catalyzed...Ch. 8 - Explain how feedback inhibition regulates...Ch. 8 - 5. Explain the lock-and-key model of enzyme...Ch. 8 - If you were to expose glucose to oxygen on your...Ch. 8 - Using what you have learned about changes in Gibbs...Ch. 8 - Prob. 10TYPSSCh. 8 - 15. The functional form of PAH contains four...
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- On the free energy diagram shown, label the intermediate (s) and transition state(s). Is the reaction thermodynamically favorable? Reaction.arrow_forwardThe following questions are based on the reaction A+ B ↔ C+D shown in Figure 8.1. 1. Which of the following terms best describes the progress of the reaction with respect to free energy change? a) endergonic, ∆G> 0 b) exergonic, ∆G> 0 c) exergonic, ∆G< 0 d) endergonic, ∆G< 0 2. Which of the following in Figure 8.1 remains unchanged by having an enzyme included? a) b b) d c) a d) c 3. The part labeled “C” on the above graph represents a) Energy of activation without enzyme b) Energy of activation with enzyme c) Amount of free energy released d) amount of energy required for the reaction progressarrow_forwardThe hydrolysis of ATP has an enthalpy and entropy of -24.3 kJ/mol and +21.6 J.K-1.mol-1, respectively, at 37 o C. What is the free energy change for the hydrolysis of 5 mols of ATP? Explain what contributes to the negative enthalpy change and positive entropy change in this reaction. What physical characteristics of the reaction would change if an ATP hydrolase enzyme is added to the solution?arrow_forward
- Of the three thermodynamic quantities, enthalpy, free energy, and entropy, which provides the most useful indicator of spontaneity in a reaction? Explain.arrow_forwardConsider the fructose-1,6-bisphosphatase reaction. Calculate the free energy change if the ratio of the concentrations of the products to the concentrations of the reactants is 23.7, and the temperature is 37.0 °C? AG" for the reaction is -16.7 kJ/mol. The constant R = 8.3145 J/(mol-K) AG= Number kJ/molarrow_forwardMetabolic pathways frequently contain reactions with positive standard free-energy values, yet the reactions still take place. How is this possible?arrow_forward
- 1) Define metabolism and describe the importance of metabolism to life. 2) Calculate the change in free energy (∆G ) for the below reaction and answer the two follow up questions: Gfinal state = 3.4 kcal/ mol and Ginitial state = 10.7 kcal/ mol Recall: ∆G = Gfinal state – Ginitial state a. Is this a spontaneous or non-spontaneous reaction? Explain. b. Is there energy released from this reaction which can be used to do work? Explain. 2) List four conditions which impact an enzymes rate of activity. Explain.arrow_forwardFind kcat for a reaction in which Vmax is 4 × 10-4 mol•min-1 and the reaction mixture contains one microgram of enzyme (the molecular weight of the enzyme is 200,000 D). Show your work/reasoning.arrow_forwardWhat do the following indicators tell you about whether a reaction can proceed as written? (a) The standard free-energy change is positive. (b) The free-energy change is positive. (c) The reaction is exergonicarrow_forward
- Label the following statements true or false: (c) A nonspontaneous reaction will proceed spontaneously in the reverse direction. (d) A spontaneous process can occur with a large decrease in entropy.arrow_forwardThe formation of maltose, a disaccharide, from two glucose molecules, is not energetically favorable. However, if this reaction is coupled with the hydrolysis of ATP, the reaction occurs more favorably. Maltose + H2O = 2 Glucose , ΔG'o = -15.5 KJ/mol or -3.7 kcal/mol a. Determine if the coupled reaction will occur spontaneously at standard state through calculating the Gibbs Free Energy of Reaction. b. Calculate the equilibrium constant for each individual reaction, and for the coupled reaction (using free energy of reaction). Show that the equilibrium constant for the coupled reaction equals the equilibrium constants for the individual reactions multiplied together. c. If the reaction medium contains the following chemical species at their given concentrations (298 K and 1.0 atm, pH = 7.0), will the reaction proceed in the forward or the reverse direction? [Maltose] = [Glucose] = 10.0 mM; [ATP] = 5.0 mM; [ADP] = [Pi] = 20 mMarrow_forwardThe following exothermic reaction is at 0.00 °C and 1.00 atm SeO4 (g) ⇌ Se(g) + O2(g) , kc = 2.4 ×10-6 The reaction contains [SeO4] = 0.100 M, [Se] = 0.0034 M, [O2] = 0.0022 M Does the reaction exist at equilibrium? If not, in what direction it will proceed? Question 22 options:arrow_forward
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