General, Organic, and Biological Chemistry Seventh Edition
General, Organic, and Biological Chemistry Seventh Edition
7th Edition
ISBN: 9781305767867
Author: H. Stephan Stoker
Publisher: Cengage Learning
bartleby

Concept explainers

Question
Book Icon
Chapter 26, Problem 26.102EP

(a)

Interpretation Introduction

Interpretation: To identify the heme degradation product (1) bilirubin, (2) biliverdin, (3) stercobilin, and (4) urobilin in whose production “ring-opening” occurs.

Concept introduction: Hemoglobin is a heme protein present in the red blood cells. The protein part is called globin and the non-protein part is heme. Heme is the prosthetic group that contains 4 pyrrole groups bonded together and has an iron atom in the center. The structure of the heme group is:

General, Organic, and Biological Chemistry Seventh Edition, Chapter 26, Problem 26.102EP , additional homework tip  1

The first step of degradation of heme involves opening of pyrrole ring with the release of the iron atom and production of biliverdin. The iron atom released becomes part of ferritin protein. Biliverdin produced is converted bilirubin in the spleen. Bilirubin is then transported to the liver where attachment of sugar residues to the propionate side chains of the bilirubin occurs to make it more soluble. Then more solubilized bilirubin is excreted in bile and finally to the small intestine. In the small intestine, it is converted into stercobilin for excretion in feces or urobilin for excretion in urine.

(b)

Interpretation Introduction

Interpretation: To identify the heme degradation product (1) bilirubin, (2) biliverdin, (3) stercobilin, and (4) urobilin in whose production a carbon-carbon double bond is changed to a carbon-carbon single bond.

Concept introduction: Hemoglobin is a heme protein present in the red blood cells. The protein part is called globin and the non-protein part is heme. Heme is the prosthetic group that contains 4 pyrrole groups bonded together and has an iron atom in the center.

The structure of the heme group is:

General, Organic, and Biological Chemistry Seventh Edition, Chapter 26, Problem 26.102EP , additional homework tip  2

The first step of degradation of heme involves opening of pyrrole ring with the release of the iron atom and production of biliverdin. The iron atom released becomes part of ferritin protein. Biliverdin produced is converted bilirubin in the spleen. Bilirubin is then transported to the liver where attachment of sugar residues to the propionate side chains of the bilirubin occurs to make it more soluble. Then more solubilized bilirubin is excreted in bile and finally to the small intestine. In the small intestine, it is converted into stercobilin for excretion in feces or urobilin for excretion in urine.

(c)

Interpretation Introduction

Interpretation: To identify the heme degradation product (1) bilirubin, (2) biliverdin, (3) stercobilin, and (4) urobilin that is rendered more water soluble by use of a glucose derivative.

Concept introduction: Hemoglobin is a heme protein present in the red blood cells. The protein part is called globin and the non-protein part is heme. Heme is the prosthetic group that contains 4 pyrrole groups bonded together and has an iron atom in the center.

The first step of degradation of heme involves opening of pyrrole ring with the release of the iron atom and production of biliverdin. The iron atom released becomes part of ferritin protein. Biliverdin produced is converted bilirubin in the spleen. Bilirubin is then transported to the liver where attachment of sugar residues to the propionate side chains of the bilirubin occurs to make it more soluble. Then more solubilized bilirubin is excreted in bile and finally to the small intestine. In the small intestine, it is converted into stercobilin for excretion in feces or urobilin for excretion in urine.

The structure of the heme group is:

General, Organic, and Biological Chemistry Seventh Edition, Chapter 26, Problem 26.102EP , additional homework tip  3

(d)

Interpretation Introduction

Interpretation: To identify the heme degradation product (1) bilirubin, (2) biliverdin, (3) stercobilin, and (4) urobilin which is bile pigment and has a yellowish color.

Concept introduction: Hemoglobin is a heme protein present in the red blood cells. The protein part is called globin and the non-protein part is heme. Heme is the prosthetic group that contains 4 pyrrole groups bonded together and has an iron atom in the center.

The structure of the heme group is:

General, Organic, and Biological Chemistry Seventh Edition, Chapter 26, Problem 26.102EP , additional homework tip  4

The first step of degradation of heme involves opening of pyrrole ring with the release of the iron atom and production of biliverdin. The iron atom released becomes part of ferritin protein. Biliverdin produced is converted bilirubin in the spleen. Bilirubin is then transported to the liver where attachment of sugar residues to the propionate side chains of the bilirubin occurs to make it more soluble. Then more solubilized bilirubin is excreted in bile and finally to the small intestine. In the small intestine, it is converted into stercobilin for excretion in feces or urobilin for excretion in urine.

Bile pigments are the colored degradation product of tetrapyrrole carbon arrangement of heme portion of hemoglobin. These are excreted in bile and give characteristic color to urine and feces.

Blurred answer
Students have asked these similar questions
Photochemical smog is formed in part by the action of light on nitrogen dioxide. The wavelength of radiation absorbed by NO2 in this reaction is 197 nm.(a) Draw the Lewis structure of NO2 and sketch its π molecular orbitals.(b) When 1.56 mJ of energy is absorbed by 3.0 L of air at 20 °C and 0.91 atm, all the NO2 molecules in this sample dissociate by the reaction shown. Assume that each absorbed photon leads to the dissociation (into NO and O) of one NO2 molecule. What is the proportion, in parts per million, of NO2 molecules in this sample? Assume that the sample behaves ideally.
Correct each molecule in the drawing area below so that it has the skeletal ("line") structure it would have if it were dissolved in a 0.1 M aqueous solution of HCI. If there are no changes to be made, check the No changes box under the drawing area. No changes. HO Explanation Check NH, 2 W O :□ G ©2025 M unter Accessibility
An expression for the root mean square velocity, vrms, of a gas was derived. Using Maxwell’s velocity distribution, one can also calculate the mean velocity and the most probable velocity (mp) of a collection of molecules. The equations used for these two quantities are vmean=(8RT/πM)1/2 and vmp=(2RT/M)1/2 These values ​​have a fixed relationship to each other.(a) Arrange these three quantities in order of increasing magnitude.(b) Show that the relative magnitudes are independent of the molar mass of the gas.(c) Use the smallest velocity as a reference for establishing the order of magnitude and determine the relationship between the larger and smaller values.

Chapter 26 Solutions

General, Organic, and Biological Chemistry Seventh Edition

Ch. 26.3 - Prob. 4QQCh. 26.3 - Prob. 5QQCh. 26.3 - Most aminotransferases are specific for the keto...Ch. 26.4 - Which of the following statements concerning the...Ch. 26.4 - Prob. 2QQCh. 26.4 - The two fuels for the urea cycle are a. carbamoyl...Ch. 26.4 - Prob. 4QQCh. 26.4 - Prob. 5QQCh. 26.4 - Prob. 6QQCh. 26.5 - Which of the following statements concerning the...Ch. 26.5 - Prob. 2QQCh. 26.5 - Prob. 3QQCh. 26.5 - Prob. 4QQCh. 26.6 - Prob. 1QQCh. 26.6 - How many of the standard amino acids are...Ch. 26.6 - The simplest pathways for amino acid biosynthesis...Ch. 26.7 - Prob. 1QQCh. 26.7 - Which of the following statements concerning the...Ch. 26.7 - Prob. 3QQCh. 26.7 - In the degradation of heme, the iron atom present...Ch. 26.8 - In degradation of the sulfur-containing amino acid...Ch. 26.8 - Prob. 2QQCh. 26.8 - Prob. 3QQCh. 26.8 - Prob. 4QQCh. 26.9 - Prob. 1QQCh. 26.9 - Prob. 2QQCh. 26.9 - Prob. 3QQCh. 26.10 - Prob. 1QQCh. 26.10 - Prob. 2QQCh. 26.10 - Prob. 3QQCh. 26 - Prob. 26.1EPCh. 26 - Indicate whether each of the following aspects of...Ch. 26 - Indicate whether each of the following pairings of...Ch. 26 - Indicate whether each of the following pairings of...Ch. 26 - Indicate whether each of the following statements...Ch. 26 - Prob. 26.6EPCh. 26 - Prob. 26.7EPCh. 26 - Prob. 26.8EPCh. 26 - Prob. 26.9EPCh. 26 - Prob. 26.10EPCh. 26 - Prob. 26.11EPCh. 26 - Prob. 26.12EPCh. 26 - Prob. 26.13EPCh. 26 - Prob. 26.14EPCh. 26 - Indicate whether each of the following situations...Ch. 26 - Indicate whether each of the following situations...Ch. 26 - Prob. 26.17EPCh. 26 - Prob. 26.18EPCh. 26 - Prob. 26.19EPCh. 26 - Prob. 26.20EPCh. 26 - Prob. 26.21EPCh. 26 - Prob. 26.22EPCh. 26 - Prob. 26.23EPCh. 26 - Prob. 26.24EPCh. 26 - Prob. 26.25EPCh. 26 - Prob. 26.26EPCh. 26 - Prob. 26.27EPCh. 26 - Prob. 26.28EPCh. 26 - Prob. 26.29EPCh. 26 - Prob. 26.30EPCh. 26 - Prob. 26.31EPCh. 26 - Prob. 26.32EPCh. 26 - Prob. 26.33EPCh. 26 - Prob. 26.34EPCh. 26 - Prob. 26.35EPCh. 26 - Prob. 26.36EPCh. 26 - Prob. 26.37EPCh. 26 - Prob. 26.38EPCh. 26 - Prob. 26.39EPCh. 26 - Prob. 26.40EPCh. 26 - Prob. 26.41EPCh. 26 - Prob. 26.42EPCh. 26 - Prob. 26.43EPCh. 26 - Draw the structure of the -keto acid produced from...Ch. 26 - Prob. 26.45EPCh. 26 - Prob. 26.46EPCh. 26 - Prob. 26.47EPCh. 26 - Prob. 26.48EPCh. 26 - Prob. 26.49EPCh. 26 - Prob. 26.50EPCh. 26 - Prob. 26.51EPCh. 26 - Prob. 26.52EPCh. 26 - Prob. 26.53EPCh. 26 - Prob. 26.54EPCh. 26 - Prob. 26.55EPCh. 26 - Prob. 26.56EPCh. 26 - Prob. 26.57EPCh. 26 - Prob. 26.58EPCh. 26 - Prob. 26.59EPCh. 26 - Prob. 26.60EPCh. 26 - Prob. 26.61EPCh. 26 - Prob. 26.62EPCh. 26 - Prob. 26.63EPCh. 26 - Prob. 26.64EPCh. 26 - Prob. 26.65EPCh. 26 - Prob. 26.66EPCh. 26 - Prob. 26.67EPCh. 26 - Prob. 26.68EPCh. 26 - Prob. 26.69EPCh. 26 - Prob. 26.70EPCh. 26 - Prob. 26.71EPCh. 26 - Prob. 26.72EPCh. 26 - Prob. 26.73EPCh. 26 - Prob. 26.74EPCh. 26 - Prob. 26.75EPCh. 26 - Prob. 26.76EPCh. 26 - Prob. 26.77EPCh. 26 - Prob. 26.78EPCh. 26 - Prob. 26.79EPCh. 26 - Prob. 26.80EPCh. 26 - Prob. 26.81EPCh. 26 - Prob. 26.82EPCh. 26 - Prob. 26.83EPCh. 26 - Prob. 26.84EPCh. 26 - Prob. 26.85EPCh. 26 - Prob. 26.86EPCh. 26 - Prob. 26.87EPCh. 26 - Prob. 26.88EPCh. 26 - Prob. 26.89EPCh. 26 - Prob. 26.90EPCh. 26 - Prob. 26.91EPCh. 26 - Prob. 26.92EPCh. 26 - Prob. 26.93EPCh. 26 - Prob. 26.94EPCh. 26 - Prob. 26.95EPCh. 26 - Prob. 26.96EPCh. 26 - Prob. 26.97EPCh. 26 - Which bile pigment is responsible for the...Ch. 26 - Prob. 26.99EPCh. 26 - Prob. 26.100EPCh. 26 - Prob. 26.101EPCh. 26 - Prob. 26.102EPCh. 26 - Prob. 26.103EPCh. 26 - Prob. 26.104EPCh. 26 - Prob. 26.105EPCh. 26 - Prob. 26.106EPCh. 26 - Prob. 26.107EPCh. 26 - Prob. 26.108EPCh. 26 - Prob. 26.109EPCh. 26 - Prob. 26.110EPCh. 26 - Prob. 26.111EPCh. 26 - Prob. 26.112EPCh. 26 - Prob. 26.113EPCh. 26 - Prob. 26.114EPCh. 26 - Prob. 26.115EPCh. 26 - Prob. 26.116EP
Knowledge Booster
Background pattern image
Chemistry
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
SEE MORE QUESTIONS
Recommended textbooks for you
Text book image
Chemistry for Today: General, Organic, and Bioche...
Chemistry
ISBN:9781305960060
Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen
Publisher:Cengage Learning
Text book image
General, Organic, and Biological Chemistry
Chemistry
ISBN:9781285853918
Author:H. Stephen Stoker
Publisher:Cengage Learning
Text book image
Organic And Biological Chemistry
Chemistry
ISBN:9781305081079
Author:STOKER, H. Stephen (howard Stephen)
Publisher:Cengage Learning,
Text book image
Introduction to General, Organic and Biochemistry
Chemistry
ISBN:9781285869759
Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres
Publisher:Cengage Learning