To determine: The overall ∆G value when it is coupled to ATP hydrolysis
The reaction is
Introduction: The full form of ATP is adenosine triphosphate, which acts as both a precursor for RNA and is known as the energy currency of the cell. The ATP is known as energy currency because the hydrolysis of ATP generates energy and power most of the endergonic reactions.
Explanation of Solution
A molecule of ATP is made up of small components such as 5-carbon sugar, ribose, which act as a framework that attaches the other subunits; another component is adenine, and triphosphate is the third component which represents a chain of three phosphates. A
The ∆G of the product (glutamine) is 3.4 kcal/mol, while the free energy released during hydrolysis of ATP is
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Chapter 6 Solutions
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- If the Go for ATP hydrolysis into ADP + inorganic phosphate is 7.3 kcal/mole, and the Go for glutamine synthesis from glutamic acid and NH3 is +3.4 kcal/mole, calculate the average Go for coupling these two reactions (glutamic acid + NH3 + ATP glutamine + ADP + inorganic phosphatearrow_forwardThe graph shows how the free‑energy change for the hydrolysis of ATP varies as a function of Mg2+ concentration. Note that pMg = –log[Mg2+]. What does the graph tell you about the relationship between Mg2+ concentration and ATP hydrolysis? What is the mechanism that explains the relationship between Mg2+ concentration and ATP hydrolysis?arrow_forwardThank you in advance!Based on the model on the picture, please help me identify these (even with no explanation):1. What is free energy? What is its symbol? 2. For an exergonic reaction, what is the value of △G? 3. For an endergonic, what is the value of △G? 4 What are the factors that affect △G? 5. What is energy coupling? In a coupling reaction, what must be the overall value of △G? 6. What does the cell do with the energy produced from exergonic reactions? 7. What molecule does the cell use as an energy carrier? Draw its structure. 8. Why is it that this energy carrier is considered to be high energy containing phosphate? 9. Bond of this energy carrier of cells is broken through what?arrow_forward
- You know that the free energy of ATP hydrolysis depends on the ATP/ADP ratio. Given that under standard conditions DGo = -30.5 kJ/mol, what should be DG of ATP hydrolysis under normal intracellular concentrations? [ATP] = 2.3 mM, [ADP] = 0.25 mM, [Pi] = 1.65 mM What is the energy of ATP hydrolysis in a cell that is ATP-depleted? [ATP] = 0.1 mM, [ADP] = 2.8 mM, [Pi] = 1.65 mMarrow_forwardRelating to bioenergetics: a. The equilibrium constant for a particular reaction is 6.8 x 10-5 which makes this reaction exergonic. True or False?b. All processes that occur in the universe are spontaneous and have low enough activation energies that molecules can often overcome the energy barrier. True or False?c. ATP has a highly negative free energy change in part because the negative charges on the oxygens repel each other in ATP but less so in ADP. True or False?arrow_forwardThe ΔG°' for hydrolysis of ATP to ADP + Pi is -30.5 kJ/mol. -Calculate the equilibrium constant for this reaction (show your work) Is this reaction at equilibrium in the cell? why?arrow_forward
- Discuss the relationship between redox potentials E0’ and the organization of the components of the electron transport chain. Be specific, i.e., use data/actual values to back up your discussion. a) What are the values of E0’ for all the components of the ETS? b)How are the E0’ related to ∆G values? c) How do the values of E0’ vary among the participants in the ETS relative to their position in the ETS?arrow_forward1. a. Calculate the physiological DG of the reaction shown below at 37°C, as it occurs in the cytosol ofneurons, with phosphocreatine at 4.7 mM, creatine at 1.0 mM, ADP at 0.73 mM, and ATP at 2.6mM. The standard free energy change for the overall reaction is –12.5 kJ/mol. Phosphocreatine + ADP ® creatine + ATP b. The enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose6-phosphate. Calculate the standard free energy change of this reaction if incubation of 20 mMglucose 1-phosphate (no glucose-6 phosphate initially present) yields a final equilibrium mixtureof 1.0 mM glucose 1-phosphate and 19 mM glucose 6-phosphate at 25°C and pH 7.0. c. If the rate of a nonenzymatic reaction is 1.2 x 10–2 μM s–1, what is the rate of the reaction at 37℃ inthe presence of an enzyme that reduces the activation energy by 30.5 kJ/mol?arrow_forwardDiscuss how Paul Boyer’s 18O exchange experiment helped to elucidate the formation of ATP by ATP Synthase. Discuss the experimental details. Chemical equations are essential. Discuss the results of his experiments. What did he expect to see? What was surprising about these results? What conclusions did he draw about the synthesis of ATP by ATP synthase?arrow_forward
- Just how much free energy is released via the passage of enough hydrogen ions through the ATP synthetase (F0F1 complex) to turn the gamma subunit (attached to the cam) TWO full 360 degrees revolutions? (0) (7) (14) (21) (42) (>42) kilocalories/mole. All choices are considered to be negative delta Gs. Briefly explainarrow_forwardA direct measurement of the standard free-energy change associated with the hydrolysis of ATP is technically demanding because the minute amount of ATP remaining at equilibrium is difficult to measure accurately. The value of ΔG′° can be calculated indirectly, however, from theequilibrium constants of two other enzymatic reactions having less favorable equilibrium constants:Using this information for equilibrium constants determined at 25 °C, calculate the standard free energy of hydrolysis of ATP.arrow_forwardDescribe in broad outline the stucture of ATP synthase(what parts make up the molecule and how are these bound in relation to each other? And how this enzyme catalyzes the synthesis of ATP mitochondriaarrow_forward
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning