Campbell Biology, Books a la Carte Plus Mastering Biology with eText -- Access Card Package (10th Edition)
10th Edition
ISBN: 9780133922851
Author: Jane B. Reece, Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Robert B. Jackson
Publisher: PEARSON
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Chapter 8.3, Problem 2CC
Summary Introduction
To determine: In which of the following there is more free energy present
Introduction: The reaction between
The free energy is more in the first reaction as the
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Write the abbreviated chemical equation for the phosphate hydrolysis reaction in the forward direction:
Glucose 3-phosphate
Write the abbreviated chemical equation for the phosphate hydrolysis reaction in the forward direction:
ATP (ADP + Pi)
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]
Chapter 8 Solutions
Campbell Biology, Books a la Carte Plus Mastering Biology with eText -- Access Card Package (10th Edition)
Ch. 8.1 - MAKE CONNECTIONS How does the second law of...Ch. 8.1 - Describe the forms of energy found in an apple as...Ch. 8.1 - WHAT IF? If you place a teaspoon of sugar in the...Ch. 8.2 - Cellular respiration uses glucose and oxygen,...Ch. 8.2 - VISUAL SKILLS How would the processes of...Ch. 8.2 - WHAT IF? Some nighttime partygoers wear glow-in-...Ch. 8.3 - How does ATP typically transfer energy from an...Ch. 8.3 - Prob. 2CCCh. 8.3 - MAKE CONNECTIONS Does Figure 8.11a show passive...Ch. 8.4 - Many spontaneous reactions occur very slowly. Why...
Ch. 8.4 - Prob. 2CCCh. 8.4 - WHAT IF? Malonate is an inhibitor of the enzyme...Ch. 8.4 - Prob. 4CCCh. 8.5 - How do an activator and an inhibitor have...Ch. 8.5 - Prob. 2CCCh. 8 - Explain how the highly ordered structure of a cell...Ch. 8 - Explain the meaning of each component in the...Ch. 8 - Describe the ATP cycle: How is ATP used and...Ch. 8 - How do both activation energy barriers and enzymes...Ch. 8 - Prob. 8.5CRCh. 8 - Choose the pair of terms that correctly completes...Ch. 8 - Prob. 2TYUCh. 8 - Which of the following metabolic processes can...Ch. 8 - Prob. 4TYUCh. 8 - Some bacteria art metabolically active in hot...Ch. 8 - If an enzyme is added to a solution where its...Ch. 8 - Prob. 7TYUCh. 8 - EVOLUTION CONNECTION Some people argue that...Ch. 8 - Prob. 9TYUCh. 8 - WRITE ABOUT A THEME: ENERGY AND MATTER Life...Ch. 8 - Prob. 11TYU
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- Consider the reaction of fructose 1,6-bisphosphate with ADP to form fructose 6-phosphate and ATP. Select the single best answer for each part. Part: 0 / 3 Part 1 of 3 Which equation shows this reaction? Part: 1/3 Part 2 of 3 ADP ATP ☑ fructose 6-phosphate fructose 1,6-bisphosphate ADP ATP fructose 1,6-bisphosphate fructose 6-phosphate ATP ADP fructose 6-phosphate fructose 1,6-bisphosphate ATP ADP fructose 1,6-bisphosphate fructose 6-phosphate If the energy change in this reaction is +3.4 kcal mol does this reaction absorb or release energy? ○ Release ○ Absorbarrow_forwardWhich of the following processes would be directly affected by the presence of a non-hydrolyzable form of ATP ? the depolymerization of tubulin monomers O the depolymerization of actin monomers the polymerization of tubulin monomers the polymerization of actin monomersarrow_forwardThe hydrolysis of the phosphoester bond of ATP releases a large amount of free energy. True or false?arrow_forward
- 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?arrow_forwardThe following molecules act as either inhibitors or activators of the enzyme that converts fructose-6-phosphate to fructose-1,6- diphosphate. Which do you think are activators? (A) ADP B AMP ATP citratearrow_forwardThe majority of glucose in the cell is in what form? (chair = chair conformation, boat=boat conformation) O a-L-glucopyranose, boat O a-D-glucopyranose, chair O B-D-glucopyranose, chair O B-D-glucopyranose, boat O B-D-glucopyranose, chair O a-D-glucopyranose, boatarrow_forward
- The protein catalase is an enzyme that catalyzes the decomposition of hydrogen peroxide:2 H2O2 (aq) → 2 H2O (l) + O2 (g)and has a Michaelis-Menten constant of 25 × 10-3 mol·dm-3 and a turnover number of 4.0×107s-1.The total enzyme concentration is 0.016×10-6 mol·dm-3 and the initial substrate concentration is4.32×10-6 mol·dm-3 Calculate the maximum reaction rate (????) for this enzyme, and the initial rateof this reaction. Note that catalase has a single active site.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 kl/mol; RT = 2.58 kJ/mol) Select one: a. -28 kJ/mol b. -33 kJ/mol C. -42 kJ/mol d. -19 kJ/molarrow_forwardEach proton that moves across the membrane releases about 14 kJ/mol of energy. Given that ATP requires 30.5 kJ/mol of energy to form, how many protons cross the membrane per ATP synthesized? (Hint: can you have half a proton?)arrow_forward
- If the ATP-binding site of an enzyme is buried in the interior of the enzyme, in a hydrophobic environment, is the ionic interaction between enzyme and substrate stronger or weaker than that same interaction would be on the surface of the enzyme, exposed to water? Why?arrow_forwardWhich one of the following is a "high-energy" biomolecule with a more negative Δ ΔG° value for hydrolysis than ATP? 1,3-Bisphosphoglycerate Fructose-1,6-Bisphosphate Dihydroxyacetone Phosphate Glucose-6-Phosphate Glycerol-1-Phosphatearrow_forwardMatch each reaction with its standard free‑energy change.arrow_forward
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