Organic Chemistry, Books a la Carte Edition (8th Edition)
Organic Chemistry, Books a la Carte Edition (8th Edition)
8th Edition
ISBN: 9780134074580
Author: Bruice, Paula Yurkanis
Publisher: PEARSON
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Chapter 22.7, Problem 12P
Interpretation Introduction

Interpretation: The reason why nitro group changes the relative leaving tendencies of carboxy and 2,4dinitrophenoxy group in the tetrahedral intermediate has to be explained.

Concept introduction:

  • Catalyst: Substance which helps in increasing the rate of a particular reaction without getting consumed in the reaction.
  • Base Catalyst: A catalyst which helps in increasing the rate of a particular reaction by the removal of a proton. There are two types of catalysis:
  1. 1. Specific-base catalysis: Proton is completely removed before the slow step in a reaction
  2. 2. General- base catalysis: Proton is completely removed during the slow step in a reaction
  • Nucleophilic catalysis: A catalysis which takes place due to the formation of a covalent bond by a nucleophile with one of the reactants.

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7. The rate constant for the hydrolysis of a m-chloro substituted and p-methoxy substituted organic substance are 0.50 and 0.015 at 25 °C, respectively. The o values of m-Cl and p-OMe are +0.37 and -0.27, respectively. Calculate the reaction constantp and rate constant for hydrolysis of unsubsituted substance and p-nitro (6 = + 0.75) substituted substance.
The following reaction follows the kinetics SN1 The substrate is: - Water - the cyanide ion - 1-ethylbenzene bromide. - 3-phenylpropanenitrile CH₂CH₂Br CN H₂O CN Since the following reaction follows an SN1 mechanism, it is correct to state: CH₂CH₂Br CH₂CH₂CN -Favors the formation of two products. -The transition state involves a pentavalent carbon. -The reaction occurs in a single step. - The first step of the reaction involves the formation of a carbocation. H2O CH₂CH₂CN
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Chapter 22 Solutions

Organic Chemistry, Books a la Carte Edition (8th Edition)

Ch. 22.9 - Which of the following amino acid side chains can...Ch. 22.9 - Which of the following C-terminal peptide bonds is...Ch. 22.9 - Carboxypeptidase A has esterase activity as well...Ch. 22.10 - Arginine and lysine side chains fit into trypsins...Ch. 22.10 - Explain why serine proteases do not catalyze...Ch. 22.11 - If H2 18O is used in the hydrolysis reaction...Ch. 22.11 - Draw the pH-activity profile for an enzyme that...Ch. 22.12 - The pHactivity profile for glucose-6-phosphate...Ch. 22.12 - Prob. 23PCh. 22.13 - Draw the mechanism for the hydroxide ion-catalyzed...Ch. 22.13 - What advantage does the enzyme gain by forming an...Ch. 22.13 - Prob. 26PCh. 22.13 - Prob. 27PCh. 22.13 - Aldolase shows no activity if it is incubated with...Ch. 22 - Which of the following parameters would be...Ch. 22 - Prob. 29PCh. 22 - Prob. 30PCh. 22 - Prob. 31PCh. 22 - Indicate the type of catalysis that is occurring...Ch. 22 - The deuterium kinetic isotope effect (KH2O/KD2O)...Ch. 22 - Prob. 34PCh. 22 - Co2+ catalyzes the hydrolysis of the lactam shown...Ch. 22 - there are two kinds of aldolases. Class I...Ch. 22 - Prob. 37PCh. 22 - The hydrolysis of the ester shown here is...Ch. 22 - Prob. 39PCh. 22 - At pH = 12, the rate of hydrolysis of ester A is...Ch. 22 - 2-Acetoxycyclohexyl tosylate reacts with acetate...Ch. 22 - Proof that an imine was formed between aldolase...Ch. 22 - Prob. 43PCh. 22 - a. Explain why the alkyl halide shown here reacts...Ch. 22 - Triosephosphate isomerase (TIM) catalyzes the...
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