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A study on oxygen binding proteins

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  1. Introduction
  2. Other biological oxygen-binding proteins
    1. Myoglobin
    2. Hemocyanin
    3. Hemerythrin
    4. Vanabins
    5. Erythrocruorin
    6. Pinnaglobin
    7. Leghemoglobin
  3. Hemoglobin
    1. Oxygen transportation
    2. Structure of hemoglobin
  4. Structure of myoglobin
  5. Structural change of hemoglobin
    1. T-R transition rate
  6. Hemoglobin and oxygen binding
    1. Quantitative description
    2. Hill plots for the binding of oxygen to hemoglobin
    3. The model for co-operative binding
    4. Two general models for the interconversion of inactive and active forms of cooperative ligand-binding protein
    5. Effect of pH on the binding of oxygen to hemo
    6. Effect of BPG on the binding of oxygen to hemoglobin
    7. Binding of BPG to deoxyhemoglobin
  7. Degradation of hemoglobin
  8. Role in disease
  9. Sickle-cell anemia is a molecular disease of hemoglobin
    1. Causes, incidence, and risk factors
    2. Symptoms
    3. Signs and tests
    4. Treatment
    5. Prevention

Myoglobin and hemoglobin may be the most-studied and best-understood proteins. They were the first protein for which three-dimensional structures were determined, and our current understanding of myoglobin and hemoglobin is garnered from the work of thousands of biochemists over several decades. Most important, they illustrate almost every aspect of biochemist processes: the reversible blinding of a ligand to a protein. This classic model of protein function will tell us a great deal about how proteins work.

Oxygen is poorly soluble in aqueous solutions and cannot be carried to tissues in sufficient quantities if it is simply dissolved in blood serum. Diffusion of oxygen through tissues is also ineffective over distances greater than few millimeters. The evolution of larger, multicellular animals depended on the evolution of protein that could transport and store oxygen. However, none of the amino acid side chains in protein is suitable for the reversible binding of oxygen molecule. This role is filled by certain transition metals, among them iron and copper, that have a strong tendency to bind oxygen.

[...] Some of these agents work by trying to induce the body to produce more fetal hemoglobin (therefore decreasing the amount of sickling) or by increasing the binding of oxygen to sickle cells. But as yet, there are no other widely used drugs that are available for treatment. Bone marrow transplants are currently the only potential cure for sickle cell anemia. In this treatment the patient's bone marrow (which makes the sickled red blood cells) is replaced with bone marrow from another individual without sickle cell disease. [...]

[...] This adjustment in the BPG level has only a small effect on the binding of oxygen in the lungs but a considerable effect on the release of oxygen in the tissues. As a result, the delivery of oxygen to the tissues is restored to nearly 40% of that which can be transported by the blood. The situation is reversed when the person returns to sea level. The BPG concentration in erythrocyte also increases the in people suffering from hypoxia, lowered oxygenation of peripheral tissues due to inadequate function of lungs or circulatory system. [...]

[...] This effect of pH and CO concentration on the binding and release of oxygen by hemoglobin is called the Bohr effect, after Christian Bhor, the Danish physiologist who discovered it in 1904. The binding equilibrium for hemoglobin and one molecule of oxygen can be designated by the reaction Hb + O2 HbO2 But this is not a complete statement. To account for the effect of concentration on this binding equilibrium, we rewrite the reaction as HHb + O HbO + H where HHb+ denotes a protonated form of hemoglobin. [...]

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