Study Guide for Campbell Biology
11th Edition
ISBN: 9780134443775
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Jane B. Reece, Martha R. Taylor, Michael A. Pollock
Publisher: PEARSON
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Chapter 8, Problem 5IQ
Summary Introduction
To explain: The reason why both the left and right sides of the given ATP cycle are examples of energy coupling.
Introduction: A series of
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The 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?
The formation of ATP by ATP Synthase is part of a coupled reaction, as
discussed in class. Given the information below and using what you know
about ATP Synthase and the proton motive force, calculate the overall AG
and determine if the coupled reaction is favorable overall. Note that you
do not need to worry about intermediates like we did for the class
example.
ADP + Pi → ATP has a AG = 7.3 kcal/mol
2 moles of protons traveling back down their gradient across the inner
mitochondrial membrane has a AG = -10.28 kcal/mol
%3D
O a. Overall AG = -17.58 kcal/mol, favorable overall
O b. Overall AG = -2.98 kcal/mol, favorable overall
%3D
O c. Overall AG = 2.98 kcal/mol, unfavorable overall
O d. Overall AG = 17.58 kcal/mol, favorable overall
Balance the following net reaction that occurs during oxidative phosphorylation. Use the smallest whole integers possible for the reaction stoichiometry.
NADH+ FADH₂ + ADP+ 0₂+H+PO, ¹
NAD+FAD+ ATP+
+H₂O
Chapter 8 Solutions
Study Guide for Campbell Biology
Ch. 8 - Complete the following concept map that summarizes...Ch. 8 - Complete the following table to indicate how the...Ch. 8 - Develop a concept map on free energy and G. The...Ch. 8 - Prob. 4IQCh. 8 - Prob. 5IQCh. 8 - In the following graph of an exergonic reaction...Ch. 8 - In the following diagram of a catalytic cycle,...Ch. 8 - Return to the diagram in Interactive Question 3.7,...Ch. 8 - Both ATP and ADP serve as regulators of enzyme...Ch. 8 - What is the relationship between the concept of...
Ch. 8 - What role do enzymes play in metabolism?Ch. 8 - ________ the totality of an organisms chemical...Ch. 8 - _______ pathways that use energy to synthesize...Ch. 8 - Prob. 3TYKFCh. 8 - _______ the most random form of energyCh. 8 - _______ term for the measure of disorder or...Ch. 8 - Prob. 6TYKFCh. 8 - _______ inhibitors that decrease an enzymes...Ch. 8 - Prob. 8TYKFCh. 8 - Prob. 9TYKFCh. 8 - Prob. 10TYKFCh. 8 - Catabolic and anabolic pathways are often coupled...Ch. 8 - Which statement most closely reflects the first...Ch. 8 - When a cell breaks down glucose, only about 34% of...Ch. 8 - Prob. 4TYKCh. 8 - Prob. 5TYKCh. 8 - Prob. 6TYKCh. 8 - One way in which a cell maintains metabolic...Ch. 8 - Prob. 8TYKCh. 8 - Prob. 9TYKCh. 8 - What is meant by an induced fit? a. The binding of...Ch. 8 - In an experiment, changing the pH from 7 to 6...Ch. 8 - Prob. 12TYKCh. 8 - Penicillin binds to the active site of an enzyme...Ch. 8 - Prob. 14TYKCh. 8 - Prob. 15TYKCh. 8 - Which line in the diagram indicates the G of the...Ch. 8 - Prob. 17TYKCh. 8 - Prob. 18TYKCh. 8 - Prob. 19TYKCh. 8 - Prob. 20TYK
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Similar questions
- Some reaction components are shown on the left. Match them to the reactions catalyzed by glutamine synthetase and glutaminase in the cell. (Multiple components on the left may match to the same option on the right. Some righthand options may have no corresponding component.) Glutamine ATP NAD+ H₂O Clear All Glutamine synthetase only Glutaminase only Both glutamine synthetase and glutaminase Neither glutamine synthetase nor glutaminasearrow_forwardExplain why some of the molecules are positioned away from the diagonal in the graph given below. What kind of processes are involved in this phenomenon? Moreover, explain differences and similarities between H-ATPases and H-PPases.arrow_forwardExplain briefly (in less than 100 words) how ATP synthase works. Show and explain the structure and function of and the difference between the two protein domains (Fo and F1) of the enzyme.arrow_forward
- Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB O a. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O b. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction O c. The enzyme stabilizes the transition state for the reaction Od. The reaction is exergonic е. The reaction is now spontaneous due to the addition of enzyme Released Energyarrow_forwardConsider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB Oa. The reaction is now spontaneous due to the addition of enzyme b. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O C. The reaction is exergonic O d. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction e. The enzyme stabilizes the transition state for the reaction Released Energy pesarrow_forwardBriefly explain the mechanism by which ATP synthase produces ATP.List three locations in which ATP synthases are found.arrow_forward
- Models such as the one shown in the illustration below are often used to represent the electron transport chain. Explain why this model is well-suited to this concept. Explain why metabolic processes such as cellular respiration and photosynthesis require a multi-stage release of energy, rather than a one-step reactionarrow_forwardThe AG of the reaction C6H12O6 + 60₂ --> 6CO₂ + 6H₂O is -686 kcal/mol glucose oxidized. The AG of the reaction ADP + P₁ --> ATP + H₂O is + 7.3 kcal/mol ATP synthesized. The oxidation of glucose can be coupled to the synthesis of ATP. If the coupling is 50% efficient, how many molecules of ATP can be synthesized per molecule of glucose oxidized? Round your answer to the nearest whole number.arrow_forwardCoupled reactions occur where a nonspontaneous reaction is enabled by coupling it to a spontaneous reaction. This approach is common in biological settings. Determine if ATP could be generated by this biochemical reaction. You have calculated that cell potential is +0.637V. An example of a coupled reaction is the first step of glycolysis, the phosphorylation of glucose to form glucose-6-phosphate shown below. The net ∆Gº for this reaction isarrow_forward
- In a biochemical pathway, three ATP molecules are hydrolyzed. The endergonic reactions in the pathway require a total of 17.3 kcal/mole of energy to drive the reactions of the pathway. What is the overall change in free energy of the biochemical pathway? Is the overall pathway endergonic or exergonic?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_forwardDetermine 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.arrow_forward
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