Becker's World of the Cell (9th Edition)
9th Edition
ISBN: 9780321934925
Author: Jeff Hardin, Gregory Paul Bertoni
Publisher: PEARSON
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Chapter 9, Problem 9.2CC
Summary Introduction
To explain: The reason for the need of using ATP as energy currency of the cell despite being intermediate energy releasing phosphorylated compound. Given
Introduction: ATP is used as the source of energy. The hydrolysis of phosphate bonds of ATP releases energy that is utilized in various biochemical processes. The interconversions, transport and other endergonic reactions require energy which is made available by ATP. The chemical energy stored as potential energy is converted into kinetic energy with the release of inorganic phosphate.
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Chapter 9 Solutions
Becker's World of the Cell (9th Edition)
Ch. 9 - How are catabolic and anabolic pathways similar?...Ch. 9 - Prob. 9.2CCCh. 9 - Why do oxidation and reduction reactions always...Ch. 9 - How can glucose be oxidized in the absence of...Ch. 9 - In the absence of oxygen, why is it necessary to...Ch. 9 - Prob. 9.6CCCh. 9 - Prob. 1QCh. 9 - Why dont glycolysis (glucose to pyruvate) and...Ch. 9 - Why are the key regulatory enzymes in glycolysis...Ch. 9 - Why do cancer cells carry out high rates of...
Ch. 9 - High-Energy Bonds. When first introduced by Fritz...Ch. 9 - The History of Glycolysis. Following are several...Ch. 9 - Glycolysis in 25 Words or Fewer. Complete each of...Ch. 9 - Energetics of Carbohydrate Utilization. The...Ch. 9 - QUANTITATIVE Glucose Phosphorylation. The direct...Ch. 9 - Ethanol Intoxication and Methanol Toxicity. The...Ch. 9 - Propionate Fermentation. Although lactate and...Ch. 9 - QUANTITATIVE Glycolysis and Gluconeogenesis. As...Ch. 9 - Prob. 9.9PSCh. 9 - Youve Got Some Explaining to Do. Explain each of...Ch. 9 - Arsenate Poisoning. Arsenate (HAsO42) is a potent...Ch. 9 - Life Without Phosphofructokinase. Many bacteria do...Ch. 9 - Prob. 9.13PS
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Similar questions
- ATP Synthase is known to catalyze the synthesis of ATP with a ΔG°’ close to zero, and a Keq' close to 1. Why is the value of ΔG°’ different from the known value which is 30.5 kJ/mol (the energy for the reverse of ATP hydrolysis)? If the Keq' value is close to one, how is it ensured that the reaction is driven to the product side and more ATP is obtained?arrow_forwardThe hydrolysis of the phosphoester bond of ATP releases a large amount of free energy. True or false?arrow_forwardIf a reaction has a ΔG°′ value of at least −30.5 kJ · mol−1, suffi -cient to drive the synthesis of ATP (ΔG°′ = 30.5 kJ · mol−1), can it still drive the synthesis of ATP in vivo when its ΔG is only −10 kJ · mol−1? Explain.arrow_forward
- If palmitic acid is subjected to complete combustion in a bomb calorimeter, one can calculate a standard free energy of combustion of 9788 kJ/mol. From the ATP yield of palmitate oxidation, what is the metabolic efficiency of the biological oxidation, in terms of kilojoules saved as ATP per kilojoule released? (Ignore the cost of fatty acid activation.)arrow_forwardCalculate the standard-state free energy change for the isomerization of glucose-1-phosphate to glucose-6-phosphatearrow_forwardIf 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_forward
- What is the significance of the ΔG°’ value of each step of Glycolysis? Why do some values classify reactions as irreversible and others as easily reversible?arrow_forwardIf the hydrolysis of 1 M glucose 6-phosphate catalyzed by glucose 6-phosphatase has a ΔG′∘ of −11.386 kJ/mol at 25 °C, what percentage of substrate remains once the reaction reaches equilibrium assuming no product was initially present? (Round answer to the nearest whole number)arrow_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
- Lactic Acid (shown below) is built up in the body during intense workouts as a result of glycolysis. Please denote if the compound is R or S. Also, explain at least two intermolecular forces it would exhibit. Would you expect this compound to be soluble in water?arrow_forwardHow many ATP will be produced in an oxidative level phosphorylation of a molecule of glucose in a eukaryotic cell?arrow_forwardWhat is a good estimate of free energy change for formation of an ES complex if the KD for this enzyme/ligand pair is 0.28µM? Give your answer in kJ/molarrow_forward
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