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, Problem 39P
Interpretation Introduction

Interpretation: The mechanism for conversion of carbon dioxide to bicarbonate ion in presence of carbonic anhydrase has to be proposed.

Concept introduction:

  • Enzyme is a protein that is a biological catalyst.  The reactant in a reaction catalyzed by the enzyme is called substrate.  In the enzyme, a pocket like cleft is present called active site where it binds the substrate.
  • Some amino acid chains in the enzyme act as base, acid and nucleophilic catalyst. Many of the enzymes contain metal ions at the active site which acts as catalyst.
  • Acid Catalyst helps in increasing the rate of a particular reaction by the donation of a proton to substrate.
  • Base Catalyst helps in increasing the rate of a particular reaction by the removal of a proton to substrate.
  • Nucleophilic catalysis helps in increasing the rate of a particular reaction by the formation of a covalent bond with substrate
  • Metalloenzyme: An enzyme which has a tightly bound Zn2+ metal ion

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The acid-base indicator HX undergoes the following reaction in a dilute aqueous solution: HX (color 1) H+ + X- (color 2). The following absorbance data were obtained for a 0.00035 M solution of HX in 0.1 M NaOH and 0.1 M HCI. Measurements were made at wavelengths of 450 nm and 620 nm using a 1.0 cm glass cuvette. 450 620 A(460 nm) A(630 nm) 0.1 M NaOH 0.1 M HCI 0.065 0.435 0.895 0.150 In the 0.1M NaOH solution, the indicator will be almost 100% in the X- form, while in 0.1M HCI, the indicator will be nearly 100% protonated (HX). Calculate the acid dissociation constant for the indicator if a pH=5 buffer solution containing a very small amount of indicator exhibits an absorbance of 0.567 at 450 nm and 0.395 at 620 nm (measured in a 1 cm glass cuvette).

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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