Modified Mastering Microbiology with Pearson eText -- Standalone Access Card -- for Brock Biology of Microorganisms (15th Edition)
15th Edition
ISBN: 9780134631530
Author: Michael T. Madigan, Kelly S. Bender, Daniel H. Buckley, W. Matthew Sattley, David A. Stahl
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Question
Chapter 3.4, Problem 1CR
Summary Introduction
Energy is nothing but ability to do work and is measured in kilojoules (KJ) unit. All
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
A) Is this reaction ( in picture provided) in equilibrium?
B) If it is not then ,what is ∆G' at 25°C if the concentration of Glucose-1-phosphate is 15.04µM and the concentration of Glucose-6-phosphate is 1.62 mM? Answer in Joules. Round to the correct number of significant figures.
(There are 103 µM in 1mM.)
Thank you so Much!!!
Consider the following chemical equation whose delta(G) = 9kcal/mol: AC + BD ---> AB + CD
what are the reactants and what are the products
is this reaction spontaneous? How do you know?
Is energy released or consumed by this reaction?
If an enzyme, which catalyzes this reaction is added, what will happen to delta (G)
If this reaction is coupled to another reaction, whose delta(G) is -12 kcal/mol, what will be the net delta(G) value?
will the overall reaction be spontaneous
Given that the standard free-energy change for the reaction glucose + Pi →glucose 6-phosphate is 13.8 kJ/mol, and the standard free-energy change forthe reaction ATP → ADP + Pi is −30.5 kJ/mol, what is the free-energychange for the reaction glucose + ATP → glucose 6-phosphate + ADP?
Chapter 3 Solutions
Modified Mastering Microbiology with Pearson eText -- Standalone Access Card -- for Brock Biology of Microorganisms (15th Edition)
Ch. 3.1 - Which four chemical elements make up the bulk of a...Ch. 3.1 - Which two classes of macromolecules contain most...Ch. 3.1 - Differentiate between trace metals and growth...Ch. 3.1 - Prob. 1CRCh. 3.2 - Compare and contrast simple transporters, the...Ch. 3.2 - Prob. 2MQCh. 3.2 - Cells of Escherichia coli transport lactose via...Ch. 3.3 - Prob. 1MQCh. 3.3 - Prob. 2MQCh. 3.3 - Prob. 1CR
Ch. 3.4 - What is free energy?Ch. 3.4 - Prob. 2MQCh. 3.4 - Using Table 3.2, calculate G0 for the reaction...Ch. 3.4 - Prob. 1CRCh. 3.5 - Prob. 1MQCh. 3.5 - Prob. 2MQCh. 3.5 - Prob. 3MQCh. 3.5 - Prob. 1CRCh. 3.6 - Prob. 1MQCh. 3.6 - Prob. 2MQCh. 3.6 - Prob. 3MQCh. 3.6 - Prob. 1CRCh. 3.7 - How much free energy is released when ATP is...Ch. 3.7 - Prob. 2MQCh. 3.7 - Prob. 3MQCh. 3.7 - Prob. 1CRCh. 3.8 - Which reactions in glycolysis are redox steps?Ch. 3.8 - Prob. 2MQCh. 3.8 - Prob. 3MQCh. 3.8 - How is ATP made in fermentation and in...Ch. 3.9 - How many molecules of CO2, NADH, and FADH2 are...Ch. 3.9 - What two major roles do the citric acid cycle and...Ch. 3.9 - Why is the glyoxylate cycle necessary for growth...Ch. 3.9 - Prob. 1CRCh. 3.10 - Prob. 1MQCh. 3.10 - Which electron carriers described in this section...Ch. 3.10 - List some of the key electron carriers found in...Ch. 3.11 - How do electron transport reactions generate the...Ch. 3.11 - How much energy is released per NADH oxidized...Ch. 3.11 - What structure in the cell links the proton motive...Ch. 3.11 - Prob. 1CRCh. 3.12 - Prob. 1MQCh. 3.12 - Prob. 2MQCh. 3.12 - Prob. 3MQCh. 3.12 - What is the major difference between aerobic...Ch. 3.13 - What form of activated glucose is used in the...Ch. 3.13 - Prob. 2MQCh. 3.13 - What functions does the pentose phosphate pathway...Ch. 3.13 - What is the importance of the enzyme...Ch. 3.14 - Prob. 1MQCh. 3.14 - List the steps required for the cell to...Ch. 3.14 - Which nitrogen bases are purines and which are...Ch. 3.14 - Prob. 1CRCh. 3.15 - Prob. 1MQCh. 3.15 - Prob. 2MQCh. 3.15 - Describe the process by which a fatty acid such as...Ch. 3 - Using the data of Figure 3.10, predict the...Ch. 3 - Prob. 2AQ
Knowledge Booster
Similar questions
- The conversion of glucose-1-phosphate to glucose-6-phosphate by the enzyme phosphoglucomutase has a △G°' of -7.6 kJ/mol. Calculate the equilibrium constant for this reaction at 298 K and a pH of 7. (R = 8.315 J/K-mol) A. 0.003 B. 0.047 C. 1.00 D. 21arrow_forwardWrite a balanced equation for each of the following reactions or reaction sequences. (a) The reaction catalyzed by PFK-2 (b) The conversion of 2 moles of oxaloacetate to glucose (c) The conversion of glucose to UDP-Glc (d) The conversion of 2 moles of glycerol toglucose (e) The conversion of 2 moles of malate to glucose-6-phosphatearrow_forwardCalculate the actual, physiological ΔG for the reaction at 37 °C, as it occurs in the cytosol of neurons, with phosphocreatine at 4.7 mM, creatine at 1.0 mM, ADP at 0.73 mM, and ATP at 2.6 mM.arrow_forward
- The free energy released by the hydrolysis of ATP under standard conditions is −30.5 kJ/mol. If ATP is hydrolyzed under standard conditions exceptat pH 5.0, is more or less free energy released? Explain.arrow_forwardIf the hydrolysis of 1 M glucose 6-phosphate catalyzed by glucose 6-phosphatase has a ΔG′∘ of −11.386 kJ/mol at 25 °C, what percentage of substrate remains once the reaction reaches equilibrium assuming no product was initially present? (Round answer to the nearest whole number)arrow_forwardConsider the following reaction: Glucose-1-phosphate → Glucose-6-phosphate ΔG° = −7.1 kJ/mol What is the equilibrium constant for this reaction at 25oC?arrow_forward
- 1. a. Calculate the physiological DG of the reaction shown below at 37°C, as it occurs in the cytosol ofneurons, with phosphocreatine at 4.7 mM, creatine at 1.0 mM, ADP at 0.73 mM, and ATP at 2.6mM. The standard free energy change for the overall reaction is –12.5 kJ/mol. Phosphocreatine + ADP ® creatine + ATP b. The enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose6-phosphate. Calculate the standard free energy change of this reaction if incubation of 20 mMglucose 1-phosphate (no glucose-6 phosphate initially present) yields a final equilibrium mixtureof 1.0 mM glucose 1-phosphate and 19 mM glucose 6-phosphate at 25°C and pH 7.0. c. If the rate of a nonenzymatic reaction is 1.2 x 10–2 μM s–1, what is the rate of the reaction at 37℃ inthe presence of an enzyme that reduces the activation energy by 30.5 kJ/mol?arrow_forwardConsider the following equilibrium at 25ºC :Glucose-1-Phosphate Glucose-6-PhophateUsing the equilibrium concentrations of [Glucose-1-Phosphate] = 0.35 M and [Glucose-6-Phosphate] = 1.65 M, calculate BOTH K′eqand Gº′ for this reaction. Is this reaction exergonicor endergonic? R = 8.314 J/K·molarrow_forwardFor the series of reactions below, what is the overall reaction and the value of ∆Go’(kJ/mol) for this set of reactions? Is the reaction spontaneous? (1) 2 Pi+ H2O ➔Pyrophosphate+ H2O (with 5 mM Mg2+) (2) (Mg)Pyrophosphate + AMP ➔(Mg)ATP (3) (Mg)ATP + creatine ➔creatine-phosphate + (Mg)ADParrow_forward
- Write a balanced equation for the complete metabolic oxidation of each of the following. Include O2, ADP, and Pi as reactants and ATP, CO2, and H2O as products. (a) Stearic acid (b) Oleic acid (c) Palmitic acid (d) Linoleic acidarrow_forwardDraw a Gibbs free energy plot for a spontaneous reaction, and then draw how enzymes affect this plot? Do enzymes change (delta)G?arrow_forwardWhy is the overall coupled reaction exergonic?arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- Human Anatomy & Physiology (11th Edition)BiologyISBN:9780134580999Author:Elaine N. Marieb, Katja N. HoehnPublisher:PEARSONBiology 2eBiologyISBN:9781947172517Author:Matthew Douglas, Jung Choi, Mary Ann ClarkPublisher:OpenStaxAnatomy & PhysiologyBiologyISBN:9781259398629Author:McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa StouterPublisher:Mcgraw Hill Education,
- Molecular Biology of the Cell (Sixth Edition)BiologyISBN:9780815344322Author:Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter WalterPublisher:W. W. Norton & CompanyLaboratory Manual For Human Anatomy & PhysiologyBiologyISBN:9781260159363Author:Martin, Terry R., Prentice-craver, CynthiaPublisher:McGraw-Hill Publishing Co.Inquiry Into Life (16th Edition)BiologyISBN:9781260231700Author:Sylvia S. Mader, Michael WindelspechtPublisher:McGraw Hill Education
Human Anatomy & Physiology (11th Edition)
Biology
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:PEARSON
Biology 2e
Biology
ISBN:9781947172517
Author:Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher:OpenStax
Anatomy & Physiology
Biology
ISBN:9781259398629
Author:McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa Stouter
Publisher:Mcgraw Hill Education,
Molecular Biology of the Cell (Sixth Edition)
Biology
ISBN:9780815344322
Author:Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter Walter
Publisher:W. W. Norton & Company
Laboratory Manual For Human Anatomy & Physiology
Biology
ISBN:9781260159363
Author:Martin, Terry R., Prentice-craver, Cynthia
Publisher:McGraw-Hill Publishing Co.
Inquiry Into Life (16th Edition)
Biology
ISBN:9781260231700
Author:Sylvia S. Mader, Michael Windelspecht
Publisher:McGraw Hill Education