Becker's World of the Cell (9th Edition)
Becker's World of the Cell (9th Edition)
9th Edition
ISBN: 9780321934925
Author: Jeff Hardin, Gregory Paul Bertoni
Publisher: PEARSON
bartleby

Concept explainers

bartleby

Videos

Textbook Question
Book Icon
Chapter 5, Problem 5.4PS

Problem Set

Enthalpy, Entropy, and Free Energy. The oxidation of glucose to carbon dioxide and water is represented by the following reaction, whether the oxidation occurs by combustion in the laboratory or by biological oxidation in living cells:

C 6 H 12 O 6 + 6 O 2 6 O 2 + 6 H 2 O     (5-27)

This reaction is highly exothermic, with an enthalpy change (ΔH) of –673 kcal/mol. As you know from Figure 5-9, ΔG for this reaction at 25°C is –686 kcal/mol, so the reaction is also highly exergonic.

(a)    Explain in your own words what the ΔH and ΔG values mean. What do the negative signs mean in each case?

(b)    What does it mean to say that the difference between the ΔG and ΔH values is due to entropy?

(c)    Without doing any calculations, would ΔS for this reaction be positive or negative? Explain your answer.

(d)    Now calculate ΔS for this reaction at 25°C. Does the calculated value agree in sign with your prediction in part c?

(e)    What are the values of ΔG, ΔH, and ΔS for the reverse of the above reaction as carried out by a photosynthetic algal cell that is using CO2 and H2O to make C6H12O6?

Chapter 5, Problem 5.4PS, Problem Set Enthalpy, Entropy, and Free Energy. The oxidation of glucose to carbon dioxide and water

Figure 5-9 Changes in Free Energy for the Oxidation and Synthesis of Glucose. The exergonic oxidation of glucose shown in (a) has a large negative ΔG that is exactly equal in magnitude but opposite in sign to the large positive ΔG for the endergonic synthesis of glucose shown in (b).

Blurred answer
Students have asked these similar questions
Kinetic Parameters of Enzyme-Catalyzed Reactions TABLE 12-1 The Values of KM, Keat, and Keat/KM for Some Enzymes and Substrates Enzyme Substrate KM (M) 9.5 x 10-5 1.2 x 10-² 2.6 x 10-2 2.5 x 10-2 4.4 x 10-1 8.8 x 10-2 6.6 x 10-4 Acetylcholinesterase Carbonic anhydrase Catalase Chymotrypsin Fumarase Urease Acetylcholine CO₂ HCO₁ H₂O₂ N-Acetylglycine ethyl ester N-Acetylvaline ethyl ester N-Acetyltyrosine ethyl ester Fumarate Malate Urea 5.0 x 10-6 2.5 x 10-5 2.5 x 10-2 Keat (S-¹) 1.4 x 104 1.0 × 106 4.0 × 105 1.0 X 107 5.1 x 10-2 1.7 × 10-1 1.9 X 10² 8.0 x 10² 9.0 × 10² 1.0 X 104 Keat/KM (M¹s¹) 1.5 × 108 8.3 x 107 1.5 x 107 4.0 X 108 1.2 x 10-1 1.9 2.9 × 105 1.6 × 108 3.6 X 107 4.0 X 105 Which enzyme is the most catalytically efficient? Which substrate does chymotrypsin bind to most tightly (assume k_₁ >> K₂)? Is fumarate or malate a better substrate of fumarase? Is it possible to have a kcat/KM of greater than 1 x 10⁹ M-¹ s-¹? Why or why not?
Matching Question: Researchers characterized a new enzyme and determined its Km=200 uM. Moreover, they found that at (Etotad10 nM this enzyme reaches maximum reaction velocity Venasa5 is 1. What is the keat of this enzyme? 2. At which concentration of the substrate this enzyme reaches initial reaction velocity (Vo) of 500 nM/s (assuming (Etotal is the same 10 nMy? 3. What is the maximum reaction velocity (Vmax) of the reaction catalyzed by this enzyme at (Etotail4 nM? Make sure to choose the correct units of measure. Note that some of the items from the answer list should NOT be used. v kcat 1. 400 uM - (S] - - Vmax 2 100 uM 500 s 450 uM 250 s1 * 501 7. so00 s 1 UM's SuMis 10 200 uM 11. 10 uMis 12 25 s 13. 500 nM/s
Initial rate data for an enzyme that obeys Michaelis–Menten kinetics areshown in the following table. When the enzyme concentration is 3 nmolml-1, a Lineweaver–Burk plot of this data gives a line with a y-intercept of0.00426 (μmol-1 ml s).                                                                                      (a) Calculate kcat for the reaction.(b) Calculate KM for the enzyme.(c) When the reactions in part (b) are repeated in the presence of 12 μM ofan uncompetitive inhibitor, the y-intercept of the Lineweaver–Burk plotis 0.352 (μmol-1 ml s). Calculate K′I for this inhibitor.
Knowledge Booster
Background pattern image
Biology
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.
Similar questions
SEE MORE QUESTIONS
Recommended textbooks for you
  • Text book image
    Biochemistry
    Biochemistry
    ISBN:9781305961135
    Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
    Publisher:Cengage Learning
    Text book image
    Biochemistry
    Biochemistry
    ISBN:9781305577206
    Author:Reginald H. Garrett, Charles M. Grisham
    Publisher:Cengage Learning
Text book image
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Text book image
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License