Use the information gathered in the Oxygen Binding Proteins Molecular Structure Tutorial to answer the question. Which five statements about hemoglobin and myoglobin structure are true? 00 By itself, heme is not a good oxygen carrier. It must be part of a larger protein to prevent a change in the oxidation state of the iron ion. Hemoglobin is a heterotetramer, whereas myoglobin is a monomer. Molecular oxygen binds reversibly to Fe2+ in heme. Each iron ion can form six coordination bonds. Two of these bonds are formed between iron and oxygen. Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron ion. Heme is composed of an organic protoporphyrin component and a metal ion. Each hemoglobin or myoglobin molecule can bind four oxygen molecules.
Use the information gathered in the Oxygen Binding Proteins Molecular Structure Tutorial to answer the question. Which five statements about hemoglobin and myoglobin structure are true? 00 By itself, heme is not a good oxygen carrier. It must be part of a larger protein to prevent a change in the oxidation state of the iron ion. Hemoglobin is a heterotetramer, whereas myoglobin is a monomer. Molecular oxygen binds reversibly to Fe2+ in heme. Each iron ion can form six coordination bonds. Two of these bonds are formed between iron and oxygen. Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron ion. Heme is composed of an organic protoporphyrin component and a metal ion. Each hemoglobin or myoglobin molecule can bind four oxygen molecules.
Introduction to General, Organic and Biochemistry
11th Edition
ISBN:9781285869759
Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres
Publisher:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres
Chapter22: Proteins
Section: Chapter Questions
Problem 22.65P: 22-65 (a) What is the difference in the quaternary structure between fetal hemoglobin and adult...
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Transcribed Image Text:Use the information gathered in the Oxygen Binding Proteins Molecular Structure Tutorial to answer the question.
Which five statements about hemoglobin and myoglobin structure are true?
By itself, heme is not a good oxygen carrier. It must be part of a larger protein to prevent a change in the oxidation state
of the iron ion.
Hemoglobin is a heterotetramer, whereas myoglobin is a monomer.
Molecular oxygen binds reversibly to Fe²+ in heme.
Each iron ion can form six coordination bonds. Two of these bonds are formed between iron and oxygen.
Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron ion.
Heme is composed of an organic protoporphyrin component and a metal ion.
Each hemoglobin or myoglobin molecule can bind four oxygen molecules.
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