Campbell Biology in Focus
3rd Edition
ISBN: 9780134710679
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Rebecca Orr
Publisher: PEARSON
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Question
Chapter 6.3, Problem 2CC
Summary Introduction
To determine:
Whether “glutamic acid + ammonia + ATP” or “glutamine + ATP +Pi” has more free energy.
Concept introduction:
Gibbs free energy is the energy present in the system that can perform work under the condition of uniform temperature and pressure. It is denoted by G.
In a
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Students have asked these similar questions
Consider the following chemical reaction:
Glucose + ATP → Glucose-6-Phosphate + ADP + Pi
Given the following information, calculate the actual free energy change (G’) of this reaction.
G’ of Glucose + ATP → Glucose-6-Phosphate + ADP + Pi = -16.7 kJ/mol
[Glucose] = 5.0 mM
[ATP] = 1.85 mM
[Glucose-6-Phosphate] = 0.083 mM
[ADP] = 0.14 mM
[Pi] = 1.0 mM Temperature = 37 C
R (Gas Constant) = 8.314 J/mol•K
As a result of an experiment following measurements were obtained from a cell: ATP concentration of 0.5 mM, ADP concentration of 0.1 mM, inorganic phosphate (Pi) concentration of 2 mM. Under these conditions calculate the actual free energy (AG) of the reaction of hydrolysis of ATP to ADP and Pi. (The standard energy (AG") of ATP = -31 kl/mol; RT = 2.58 kJ/mol)
Select one:
a. -28 kJ/mol
b. -33 kJ/mol
C. -42 kJ/mol
d. -19 kJ/mol
The hydrolysis of the disaccharide sucrose results in the formation of the
monosaccharides glucose and fructose, and the AG of this reaction is -29.3 kJ/mol.
Sucrase is an enzyme that is able to catalyze the hydrolysis of sucrose. Which of the
following statement(s) correctly describes what would happen if you added the
enzyme sucrase to a solution of sucrose?
All of the other three statements are correct.
The activation energy of the reaction would increase.
The AG of the reaction would become more negative (i.e., a larger negative
number).
The rate of sucrose hydrolysis would increase.
Chapter 6 Solutions
Campbell Biology in Focus
Ch. 6.1 - MAKE CONNECTIONS How does the second law of...Ch. 6.1 - Describe the forms of energy found in an apple as...Ch. 6.2 - Cellular respiration uses glucose and oxygen,...Ch. 6.2 - Prob. 2CCCh. 6.2 - Prob. 3CCCh. 6.3 - How does ATP typically transfer energy from...Ch. 6.3 - Prob. 2CCCh. 6.3 - MAKE CONNECTIONS Does Figure 6.10a show passive or...Ch. 6.4 - Many spontaneous reactions occur very slowly. Why...Ch. 6.4 - Why do enzymes act only on very specific...
Ch. 6.4 - WHAT IF? Malonate is an inhibitor of the enzyme...Ch. 6.4 - A mature lysosome has an internal pH of around...Ch. 6.5 - How do an activator and an inhibitor have...Ch. 6.5 - Prob. 2CCCh. 6 - Choose the pair of terms that correctly completes...Ch. 6 - Prob. 2TYUCh. 6 - Which of the following metabolic processes can...Ch. 6 - If an enzyme in solution is saturated with...Ch. 6 - Some bacteria are metabolically active in hot...Ch. 6 - If an enzyme is added to a solution where its...Ch. 6 - DRAW IT Using a series of arrows, draw the...Ch. 6 - Prob. 8TYUCh. 6 - SCIENCE, TECHNOLOGY, AND SOCIETY Organophosphates...Ch. 6 - FOCUS ON EVOLUTION A recent revival of the...Ch. 6 - FOCUS ON ENERGY AND MATTER Life requires energy....Ch. 6 - SYNTHESIZE YOUR KNOWLEDGE Explain what is...
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Similar questions
- Consider the following reaction: Glucose + ATP Glucose 6-phosphate + ADP This reaction has a AG'° = -16.7 kJ/mol. In a cell, it has a AG = -33.4 kJ/mol. Which of the following would make AG less than (more negative than) AG'°? (Pick two.) [ATP] > [ADP] [ATP] [Glucose 6-phosphate] < [Glucose] [Glucose 6-phosphate]arrow_forwardGastric juice (pH 1.5) is produced by pumping HCl from blood plasma (pH 7.4) into the stomach. Calculate the amount of free energy required to concentrate the H+ in 1 L of gastric juice at 37 °C. Under cellular conditions,how many moles of ATP must be hydrolyzed to provide this amount of free energy? The free-energy change for ATP hydrolysis under cellular conditions is about −58 kJ/mol . Ignore the effects of the transmembrane electrical potential.arrow_forwardA critical reaction in the production of energy to do work or drive chemical reactions in biological systems is the hydrolysis of adenosine triphosphate, ATP, to adenosine diphosphate, ADP, as described by the reaction ATP(aq)+H2O(l)⟶ADP(aq)+HPO2−4(aq)ATP(aq)+H2O(l)⟶ADP(aq)+HPO42−(aq) for which Δ?∘rxn=−30.5 kJ/molΔGrxn∘=−30.5 kJ/mol at 37.0 °C and pH 7.0. Calculate the value of Δ?rxnΔGrxn in a biological cell in which [ATP]=5.0 mM,[ATP]=5.0 mM, [ADP]=0.10 mM,[ADP]=0.10 mM, and [HPO2−4]=5.0 mM.[HPO42−]=5.0 mM. Δ?rxn=ΔGrxn= kJ/molarrow_forward
- G6P(ag) F6P(aq) AG°=+1.7kJ/mol at 25 °C Consider the reaction: Estimate the fraction of F6P (Fructose 6 Phosphate) in equilibrium with G6P (Glucose 6 Phosphate) at 25 °C, where the fraction is defined as [F6P]/([F6P]+[G6P]). Show ALL your work.arrow_forwardWhat is the ∆G naught' for a phosphoryl transfer from ATP to glycerol? The hydrolysis of α-glycerophosphate to glycerol and inorganic phosphate has a ∆G naught' of -8.37 kj/mol. ATP + H2O <--> ADP + Pi ∆G naught' = -30.5 kj/mol What is the efficiency of this reaction (i.e. what % of the available energy remains in the system after the reaction)? Express your answer as a % of the total amount of energy available in the system. Where does the rest of the energy go?arrow_forwardAs a result of an experiment following measurements were obtained from a cell: ATP concentration of 0.5 mM, ADP concentration of 0.1 mM, inorganic phosphate (Pi) concentration of 2 mM. Under these conditions calculate the actual free energy (AG) of the reaction of hydrolysis of ATP to ADP and Pi. (The standard energy (AG°) of ATP = -31 kJ/mol; RT = 2,58 kJ/mol) Select one: O a. -28 kJ/mol O b. -33 kJ/mol OC. -19 kJ/mol O d. -42 kJ/molarrow_forward
- What is the standard free-energy change, ∆G°, under physiological conditions(E. coli grows in the human gut, at 37 °C) for the following reaction?Glucose + ATP → glucose 6-phosphate + ADParrow_forwardIn the reaction ATP + glucose → ADP + glucose-6-phosphate, ΔG° is -16.7 kJ/mol. Assume that both ATP and ADP have a concentration of 1 M and T = 25°C. What ratio of glucose-6- phosphate to glucose would allow the reverse reaction to occur?arrow_forwardConsider an enzyme (P) that gets activated by forming a dimer (P2): 2P = P2 At 25 °C, we have AH- 19 kJ/mol and AS-65 kJ/mol, for this dimerization reaction. Identify the correct statement. O The enzyme is activated when kept at temp = +37 °C. O The enzyme is activated at all temperatures. O The enzyme is activated when kept in the fridge with temp = 4 "C. O The enzyme can never be activated, no matter what the temperature is. O None of the above statements is true.arrow_forward
- Write the abbreviated chemical equation for the phosphate hydrolysis reaction in the forward direction: ATP (ADP + Pi)arrow_forwardThe enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose 6-phosphate. After the reactants and products were mixed and allowed to reach equilibrium at 25°C, the concentration of glucose 1-phosphate was 4.5 mM and that of glucose 6-phosphate was 86 mM. Calculate Keq' and AG for this reaction. The reaction coordinate diagram for an enzyme-catalyzed reaction is shown below. How many transition states and intermediates are in the reaction? Is the reaction thermodynamically favorable? Which step is the rate-determining step of the reaction? G Reaction coordinatearrow_forwardWrite the abbreviated chemical equation for the phosphate hydrolysis reaction in the forward direction: Glucose 3-phosphatearrow_forward
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