Biochemistry
9th Edition
ISBN: 9781305961135
Author: Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher: Cengage Learning
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Chapter 15, Problem 25RE
RECALL For each of the reactions in Question 24, give the oxidizing agent and reducing agents.
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Calculate the isoelectronic point, pl, from the pKa values for histidine, arginine and asparagine.
The free energy released by the hydrolysis of ATP under standard conditions is -30.5 kJ/mol.
If ATP is hydrolyzed under standard conditions except at pH 5.0, is more or less free energy released? Why?
More free energy is released because the increased [H+] stabilizes the negative charge on the ADP molecule.
Less free energy is released because an acidic environment depletes cellular ATP levels.
Less free energy is released because the reaction favors ATP production over hydrolysis due to the higher [H+]
in solution.
More free energy is released because the total cellular concentrations of ATP, ADP, and P; are greater at the lower
pH.
Correct Answer
Consider a system consisting of an egg in an incubator. The white and yolk of the egg contain proteins, carbohydrates, and
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How does the entropy change in both the system (developing chick) and suroundings (the egg environment) drive the
irreversible process of chick development?
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The release of glucose from sucrose, which produces energy needed for chick development, decreases entropy in
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Chick development increases entropy in the system, which causes a concominant decrease in entropy in
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Carbohydrates, proteins, and lipids within the egg break down into CO2 and H2O, which increases entropy in
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Chick development decreases entropy in the system, but this is smaller than the concominant increase in entropy in
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Chapter 15 Solutions
Biochemistry
Ch. 15 - RECALL Is there a connection between the...Ch. 15 - REFLECT AND APPLY What do the following indicators...Ch. 15 - REFLECT AND APPLY Consider the reaction...Ch. 15 - RECALL What conditions are necessary for the...Ch. 15 - REFLECT AND APPLY Why is it important that energy...Ch. 15 - RECALL Why is it necessary to define a modified...Ch. 15 - RECALL Which of the following statements is (are)...Ch. 15 - RECALL How can you tell if the standard Gibbs free...Ch. 15 - RECALL Can the thermodynamic property G be used to...Ch. 15 - MATHEMATICAL Calculate G for the following values...
Ch. 15 - Prob. 11RECh. 15 - MATHEMATICAL Consider the reaction AB+C, where...Ch. 15 - Prob. 13RECh. 15 - MATHEMATICAL The G for the reaction Citrate ...Ch. 15 - MATHEMATICAL If a reaction can be written AB, and...Ch. 15 - Prob. 16RECh. 15 - Prob. 17RECh. 15 - Prob. 18RECh. 15 - RECALL Organize the following words into two...Ch. 15 - Prob. 20RECh. 15 - REFLECT AND APPLY Would you expect the production...Ch. 15 - Prob. 22RECh. 15 - REFLECT AND APPLY Adult humans synthesize large...Ch. 15 - RECALL Identify the molecules oxidized and reduced...Ch. 15 - RECALL For each of the reactions in Question 24,...Ch. 15 - Prob. 26RECh. 15 - RECALL What is the structural difference between...Ch. 15 - RECALL How does the difference between NADH and...Ch. 15 - RECALL Which coenzyme is a reactant in the...Ch. 15 - Prob. 30RECh. 15 - Prob. 31RECh. 15 - Prob. 32RECh. 15 - REFLECT AND APPLY The following half reactions...Ch. 15 - Prob. 34RECh. 15 - REFLECT AND APPLY There is a reaction in...Ch. 15 - REFLECT AND APPLY There is a reaction in which...Ch. 15 - Prob. 37RECh. 15 - Prob. 38RECh. 15 - Prob. 39RECh. 15 - Prob. 40RECh. 15 - MATHEMATICAL Using the data in Table 15.1,...Ch. 15 - Prob. 42RECh. 15 - Prob. 43RECh. 15 - MATHEMATICAL The standard free-energy change for...Ch. 15 - Prob. 45RECh. 15 - Prob. 46RECh. 15 - Prob. 47RECh. 15 - REFLECT AND APPLY Would you expect an increase or...Ch. 15 - REFLECT AND APPLY Explain and show why...Ch. 15 - Prob. 50RECh. 15 - Prob. 51RECh. 15 - Prob. 52RECh. 15 - Prob. 53RECh. 15 - REFLECT AND APPLY Why are thioesters considered...Ch. 15 - Prob. 55RECh. 15 - REFLECT AND APPLY This is a conjectural question:...
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- The amino acid glycine is often used as the main ingredient of a buffer in biochemical experiments. The amino group of glycine, which has a pKa of 9.6, can exist either in the protonated form -NH or as the free base -NH2, because of the reversible equilibrium R-NH =R-NH₂ + H+ In what pH range can glycine be used as an effective buffer due to its amino group? pH 8.6 to pH 10.6 In a 0.1 M solution of glycine at pH 9.0, what fraction of glycine has its amino group in the -NH form? Correct Answer Correct Answer 45 How much 5 M KOH must be added to 1.0 L of 0.1 M glycine at pH 9.0 to bring its pH to 10.0? 10 mL When 99% of the glycine is in its -NH form, what is the numerical relation between the pH of the solution and the pKa of the amino group? pH = pKa - 2 Correct Answer Correct Answerarrow_forwardThe glycolytic enzyme Phosphofructokinase (PFK) catalyzes the following reaction: Fructose-6-phosphate (F6P) + ATP → Fructose-1,6-bisphosphate (F1,6BP) + ADP AG"=-14.2 kJ/mol This is considered the enzymatic step that commits a sugar substrate to glycolysis. a) Calculate the standard free energy of hydrolysis of fructose-1,6-bisphosphate. b) What is the equilibrium constant for this coupled reaction? c) ATP is a known inhibitor of PFK. If the cellular concentrations of ATP and ADP are 5 mM and 1.0mM respectively, and the concentrations of F6P and F1,6BP are 2mM, what is the free energy change of the system?arrow_forward2) Consider the following reaction: A + 2B 3C + D At equilibrium the concentration of the reactants and products are: [A] = 20.0 mM [C] = 3.0 mM [B] = 4.0 mM [D] = 50.0 mM Calculate (a) the equilibrium constant and (b) AG". Comment on which side of this reaction is more likely to occur.arrow_forward
- Glycine is a diprotic acid, which can potentially undergo two dissociation reactions, one for the a-amino group (NH), and the other for the carboxyl (-COOH) group. Therefore, it has two pK₁ values. The carboxyl group has a pK₁ of 2.34 and the α-amino group has a pK2 of 9.60. Glycine can exist in fully deprotonated (NH2-CH2-COO¯), fully protonated (NH3-CH2-COOH), or zwitterionic form (NH3-CH2-COO¯). Match the pH values with the corresponding form of glycine that would be present in the highest concentration in a solution of that pH. fully deprotonated form NH2-CH2-COO- fully protonated form NH–CH,–COOH zwitterionic form NH–CH,−COO Answer Bank pH 7.0 pH 11.9 pH 6.0 pH 8.0 pH 1.0arrow_forwardThe AG of hydrolysis of a sugar phosphate (S-O-P) to the free sugar (S-OH) is -26.6 kJ/mol in a hypothetical cell in which the steady-state concentrations of sugar phosphate, free sugar, and inorganic phosphate are 1.0 mM, 0.20 mM, and 50.0 mM, respectively. S-O-P + H2O S-OH + Pi (a) What is the AG°' for this reaction? (b) In the cell, S-O-P is formed by the transfer of a phosphate group from ATP. What would the AG be for the transfer of the g-phosphate from ATP to this sugar (S-OH)? [AG for ATP hydrolysis is -31 kJ/mol.]arrow_forward1) Consider the reaction: A B + C (a) What is the Keg for this reaction? AG= -8.80 kJ/mol (b) The reverse reaction is initiated by creating a solution containing 20mM B, 1mM A and 150mM C. At the instant these are mixed, what is the free energy change associated with the reaction?arrow_forward
- What is the chemical importance of the negative charge on the phosphate group? Be asspecific as possible. In what ways might this negative charge have beenthermodynamically useful during the evolution of ATP-binding proteins?arrow_forwardOne prominent theory on life origins was that RNA enzymes came into existence early inthe prebiotic history of Earth and were able to do basic chemical catalyses. Eventually,this “RNA-world” was overtaken by the stability of DNA as an information carrier and thediversity of catalytic functions capable of being performed by polypeptides. Is the RNA world hypothesis is a well-founded model?arrow_forwardThe AG" of hydrolysis (ATP + H2O --> ADP + Pi) is -31.0 kJ/mol. Answer the following questions assuming that the steady-state concentrations in the cell are as indicated below. (Note: Steady-state refers to a non-equilibrium situation that exists due to a balance between reactions that supply and remove these substances.) [ADP] = 0.40 mM, [ATP] = 4.0 mM, and [Pi] = 40.0 mM a) Calculate the equilibrium constant for this reaction. b) What would the AG' for ATP hydrolysis be in the cell? c) Is this reaction at equilibrium in the cell? Briefly explain your answer.arrow_forward
- 5) Theoretically, ATP did not have to become our bodies' main energy currency. Two alternative carriers, acetyl phosphate and S-adenosylmethionine could have been utilized, rather than ATP. AG" for acetyl phosphate hydrolysis is -43.3 kJ/mol and AG" for S- adenosylmethionine hydrolysis is -25.6 kJ/mol. (a) Calculate the weight of each alternative energy carrier that would need to be consumed by humans on a 2000 calorie per day diet if our bodies could not recycle it. Assume a 50% absorption of energy from our diet. (b) If our bodies contain 25g of each alternative energy carrier and they CAN be recycled, how many times would each molecule of each energy carrier need to be recycled? (c) Comment on the special properties of ATP and why it is unlikely that these alternative carriers would be utilized biologically.arrow_forwardGive three reasons why evolution may have selected for phosphates compared to othersimilar leaving groups such as conjugated carboxylic acids or amides. Explain whatbenefit each of your reasons has granted to the living organism.arrow_forwardThe preferred substrate is T because the enzyme half-saturates at 7.00 mM for T, but requires 28.0 mM for U, and 112 mM for S. b Question Content Area The rate constant k 2 with substrate S is 9.60×107 sec-1, with substrate T, k 2 = 6.00×104 sec-1, and with substrate U, k 2 = 2.40×106 sec-1. Calculate the catalytic efficiency with S, T, and U. Catalytic efficiency with S = Catalytic efficiency with T = Catalytic efficiency with U = Does enzyme A use substrate S, substrate T, or substrate U with greater catalytic efficiency?arrow_forward
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