Organic Chemistry
9th Edition
ISBN: 9781305080485
Author: John E. McMurry
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Concept explainers
Textbook Question
Chapter 6.SE, Problem 18VC
Look at the following energy diagram for an enzyme-catalyzed reaction:
(a) How many steps are involved?
(b) Which step is most exergonic?
(c) Which step is slowest?
Expert Solution & Answer
Trending nowThis is a popular solution!
Students have asked these similar questions
In a multi-step reaction pathway, the
step is the rate-limiting step.
(A)
(B)
Fastest
Slowest
Enzymes are remarkably efficient catalysts that can increase reaction rates by as many as 20 orders of magnitude.(a) How does an enzyme affect the transition state of a reac-tion, and how does this effect increase the reaction rate?(b) What characteristics of enzymes give them this tremendous effectiveness as catalysts?
Consider the simple reaction S <--> P, with the forward rate characterized by a rate constant k1, the reverse rate constant characterized by a rate constant k2, and the equilibrium constant for the reaction given by Keq. Which of the listed effects would be brought about by an enzyme catalyzing this reaction?a) increased Keqb) increased k1c) decreased transition state free energy changed) increased k2
Chapter 6 Solutions
Organic Chemistry
Ch. 6.1 - Prob. 1PCh. 6.3 - Prob. 2PCh. 6.3 - Using curved fishhook arrows, propose a mechanism...Ch. 6.4 - Prob. 4PCh. 6.4 - An electrostatic potential map of boron...Ch. 6.5 - What product would you expect from reaction of...Ch. 6.5 - Reaction of HBr with 2-methylpropene yields...Ch. 6.6 - Prob. 8PCh. 6.6 - Predict the products of the following polar...Ch. 6.7 - Which reaction is more energetically favored, one...
Ch. 6.7 - Prob. 11PCh. 6.9 - Which reaction is faster, one with ∆G‡ = +45...Ch. 6.10 - Prob. 13PCh. 6.SE - Prob. 14VCCh. 6.SE - Prob. 15VCCh. 6.SE - Prob. 16VCCh. 6.SE - Look at the following energy diagram: (a) Is...Ch. 6.SE - Look at the following energy diagram for an...Ch. 6.SE - What is the difference between a transition state...Ch. 6.SE - Prob. 20EDRMCh. 6.SE - Prob. 21EDRMCh. 6.SE - Draw an energy diagram for a two-step exergonic...Ch. 6.SE - Draw an energy diagram for a reaction with keq =...Ch. 6.SE - The addition of water to ethylene to yield ethanol...Ch. 6.SE - When isopropylidenecyclohexane is treated with...Ch. 6.SE - Prob. 26EDRMCh. 6.SE - Draw the electron-pushing mechanism for each...Ch. 6.SE - Draw the complete mechanism for each polar...Ch. 6.SE - Prob. 29EDRMCh. 6.SE - Identify the functional groups in the following...Ch. 6.SE - Identify the following reactions as additions,...Ch. 6.SE - Identify the likely electrophilic and nucleophilic...Ch. 6.SE - For each reaction below identify the electrophile...Ch. 6.SE - Prob. 34APCh. 6.SE - Follow the flow of electrons indicated by the...Ch. 6.SE - Prob. 36APCh. 6.SE - Prob. 37APCh. 6.SE - Despite the limitations of radical chlorination of...Ch. 6.SE - Prob. 39APCh. 6.SE - Answer question 6-39 taking all stereoisomers into...Ch. 6.SE - Prob. 41APCh. 6.SE - Prob. 42APCh. 6.SE - Prob. 43APCh. 6.SE - The reaction of hydroxide ion with chloromethane...Ch. 6.SE - Prob. 45APCh. 6.SE - Ammonia reacts with acetyl chloride (CH3COCl) to...Ch. 6.SE - The naturally occurring molecule α-terpineol is...Ch. 6.SE - Prob. 48APCh. 6.SE - Prob. 49APCh. 6.SE - Draw the structures of the two carbocation...
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.Similar questions
- True or false: When the temperature of an exothermicreaction increases, the rate constant of the forward reactiondecreases, which leads to a decrease in the equilibriumconstant, Kc.arrow_forwardac cic with equal ease? 4 Compare the activation energy in uncatalyzed reac- tions and in enzyme-catalyzed reactions. q 190 WIL nood in many differentarrow_forward017) litre n of r is 8. Which one of the following statements is incorrect about enzyme catalysis? (a) Enzymes are mostly proteinous in nature. (b) Enzyme action is specific. (c) Enzymes are denatured by ultraviolet rays and at high temperature. (d) Enzymes are least reactive at optimum temperature. 201 15. Accor catalys becaus (a) the the higarrow_forward
- Aldolase catalyzes the glycolytic reaction The standard free-energy change for this reaction in the direction written is +23.8 kJ/mol. The concentrations of the three intermediates in the hepatocyte of a mammal are: fructose 1,6-bisphosphate, 1.4 × 10−5 M; glyceraldehyde 3-phosphate, 3 × 10−6 M; and dihydroxyacetone phosphate, 1.6 ×10−5 M. At body temperature (37 °C), what is the actual free-energy change for the reaction?arrow_forwardOur body obtains energy from the combustion of glucose. During this process, glycerate is transformed first into pyruvate. This reaction has an activation energy close to 44 kJ. Estimate how many times faster this reaction is when someone has a high fever close to 106 F (41 oC) compared to its rate at normal body temperature (98.6 F; 37 oC). Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer. a b с d 31% faster 11% faster 24% faster 259% faster Your answerarrow_forwardThe rate law for the reaction NO₂ (g)+CO(g) → NO(g)+CO₂ (g) is rate k[NO₂]² ; one possible mechanism is shown on p. 717.(a) Draw a reaction energy diagram for that mechanism, giventhat ΔH°overall =-226 kJ/mol.(b) Consider the following alternative mechanism:Is the alternative mechanism consistent with the rate law? Isone mechanism more reasonable physically?arrow_forward
- 36. The gas-phase reaction H+ D2 → HD + D is the exchange of isotopes of hydrogen of atomic mass 1 (H) and 2 (D, deuterium). The following data were obtained for the rate constant k of this reaction: Temperature (K) k (L mol-1 s-1) 299 1.56 x 104 327 3.77 x 104 346 7.6 x 104 440 106 549 1.07 × 105 745 8.7 x 107arrow_forward(d) On the other hand, in quantum physics/mechanics/chemistry, energy is assumed to be quantized and distributed. Therefore, virtually any reaction can take place in a cell even though some reactions remain exceedingly slow (or not possible on the time-scale of life processes) without enzyme catalysis. Explain why.arrow_forwardWhat do you predict the addition of an acid will have on catalase? Will it increase, decrease, or have no effect on the chemical reaction between hydrogen peroxide and catalase?arrow_forward
- (2) net energy change potential energy of the reactants potential energy of the products (1) (3) activation energy (4) Reaction pathway Potential energyarrow_forward4. D) True or False: In order for a catalyst to function, it must exist in the same phase as the substrate.arrow_forwardIf you add enzyme to a solution containing only the product(s) of a reaction, would you expect any substrate to form? No, because the enzyme lowers the transition state energy barrier. Yes, because the reaction proceeds backwards until reaching equilibrium. Yes, because the enzyme reduces the standard free energy change for the reaction. No, because enzymes catalyze only the forward reaction. No, because the product inhibits the enzyme.arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- Chemistry for Today: General, Organic, and Bioche...ChemistryISBN:9781305960060Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. HansenPublisher:Cengage LearningIntroductory Chemistry: A FoundationChemistryISBN:9781337399425Author:Steven S. Zumdahl, Donald J. DeCostePublisher:Cengage LearningChemistry: The Molecular ScienceChemistryISBN:9781285199047Author:John W. Moore, Conrad L. StanitskiPublisher:Cengage Learning
Chemistry for Today: General, Organic, and Bioche...
Chemistry
ISBN:9781305960060
Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen
Publisher:Cengage Learning
Introductory Chemistry: A Foundation
Chemistry
ISBN:9781337399425
Author:Steven S. Zumdahl, Donald J. DeCoste
Publisher:Cengage Learning
Chemistry: The Molecular Science
Chemistry
ISBN:9781285199047
Author:John W. Moore, Conrad L. Stanitski
Publisher:Cengage Learning
Enzymes - Effect of cofactors on enzyme; Author: Tutorials Point (India) Ltd;https://www.youtube.com/watch?v=AkAbIwxyUs4;License: Standard YouTube License, CC-BY
Enzyme Catalysis Part-I; Author: NPTEL-NOC IITM;https://www.youtube.com/watch?v=aZE740JWZuQ;License: Standard Youtube License