The list of all the modulators of oxygen binding by hemoglobin discussed in the given chapter is to be stated. The way by which the given modulators enhance the function of hemoglobin under physiological conditions is to be stated. Whether any of the modulator of hemoglobin also functions similarly in myoglobin or not is to be stated. The reason corresponding to the correct choice is to be stated. Concept introduction: Proteins are the biomolecules which are composed of the long chain of amino acid residues. The protein which contains oxygen and is present in the red blood cells in the body is known as hemoglobin. It contains iron as well. The protein that is an oxygen and iron containing protein present in the muscle tissue of mammals is known as myoglobin.

Question

The primary and tertiary structures of hemoglobin and myoglobin are very similar and both contain the 'heme' group as an oxygen-binding prosthetic group. However this There are important functional differences between the two proteins. Hemoglobin oxygen transport protein, myoglobin functions as oxygen storage protein. Hemoglobin and consider the structural differences and oxygen binding curves between myoglobin why myoglobin is a good oxygen transport protein, while hemoglobin Explain why it cannot be a good oxygen storage protein.

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Chapter 7, Problem 20P

Interpretation Introduction

Interpretation:

The list of all the modulators of oxygen binding by hemoglobin discussed in the given chapter is to be stated. The way by which the given modulators enhance the function of hemoglobin under physiological conditions is to be stated. Whether any of the modulator of hemoglobin also functions similarly in myoglobin or not is to be stated. The reason corresponding to the correct choice is to be stated.

Concept introduction:

Proteins are the biomolecules which are composed of the long chain of amino acid residues. The protein which contains oxygen and is present in the red blood cells in the body is known as hemoglobin. It contains iron as well. The protein that is an oxygen and iron containing protein present in the muscle tissue of mammals is known as myoglobin.

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The primary and tertiary structures of hemoglobin and myoglobin are very similar and both contain the 'heme' group as an oxygen-binding prosthetic group. However this There are important functional differences between the two proteins. Hemoglobin oxygen transport protein, myoglobin functions as oxygen storage protein. Hemoglobin and consider the structural differences and oxygen binding curves between myoglobin why myoglobin is a good oxygen transport protein, while hemoglobin Explain why it cannot be a good oxygen storage protein.

Red blood cells synthesize and degrade 2,3-biphosphogylerate (2,3-BPG) as a detour from the glycolytic pathway, as shown in the figure.2,3-BPG decreases the oxygen affinity of hemoglobin by binding in the central cavity of the deoxygenated form of hemoglobin. This encourages delivery of oxygen to tissues. A defect in one of the glycolytic enzymes may affect levels of 2,3-BPG. The plot above right shows oxygen-binding curves for normal erythrocytes and for hexokinase and pyruvate kinase-deficient erythrocytes. Identify which curve corresponds to which enzyme deficiency.

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