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

What is the role of 2, 3-Bisphosphoglycerate (2,3-BPG) in the function of haemoglobin as an oxygen carrier molecule? Explain the binding mechanism and effect of 2,3-BPG leading to the reduced oxygen binding affinity for haemoglobin and transitions in the T (deoxygenated) and R (oxygenated) states of haemoglobin.

Answer 1

Question

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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What is the role of 2, 3-Bisphosphoglycerate (2,3-BPG) in the function of haemoglobin as an oxygen carrier molecule? Explain the binding mechanism and effect of 2,3-BPG leading to the reduced oxygen binding affinity for haemoglobin and transitions in the T (deoxygenated) and R (oxygenated) states of haemoglobin.

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.

Suppose you mutate the proximal histidine of hemoglobin to glycine. You study the behavior of this mutant hemoglobin in the presence of 10 mM imidazole; the imidazole molecule can substitute for the proximal histidine chain and bind to the heme iron just as histidine does. a) Which state (T or R) will this mutation favor? b) Will oxygen binding to this state be tighter or weaker than oxygen binding to the same state of the wildtype hemoglobin? (note: wildtype means refers to the phenotype of the typical form of a species as it occurs in nature) c) Will this mutant still display significant cooperativity (Please provide clear and sufficient explanation for each part, thank you!)