Oxygen Dissociation Curves

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Transport of Oxygen
Oxygen is carried in red blood cells bound to haemoglobin. The haemoglobin molecule consists of four polypeptide chains, with a haem prosthetic group at the centre of each chain. Each haem group contains one iron atom, and one oxygen molecule binds to each iron atom. So one haemoglobin molecule can bind up to 4 oxygen molecules. This means there are 4 binding steps, as shown in this chemical equation:

Oxygen dissociation curve

The oxygenhaemoglobin dissociation curve plots the proportion of haemoglobin in its saturated form on the vertical axis against the prevailing oxygen tension on the horizontal axis. The oxyhaemoglobin dissociation curve is an important tool for understanding how our blood carries and releases oxygen.

 In its most simple form, the oxyhaemoglobin dissociation curve describes the relation between the partial pressure of O2 (x axis) and the oxygen saturation (y axis). Haemoglobin's affinity for oxygen increases as successive molecules of oxygen bind. More molecules bind as the oxygen partial pressure increases until the maximum amount that can be bound is reached. As this limit is approached, very little additional binding occurs & the curve levels out as the haemoglobin becomes saturated with O2. Hence the curve has a sigmoidal or S-shape. The further to the left the curve, the greater is the affinity of haemoglobin for oxygen (so it takes up oxygen readily but releases it less easily). The further to the right the curve, the lower is the affinity of haemoglobin for oxygen (so it takes up oxygen less readily but releases it more easily).

Effect of CO2 Concentration

Hemoglobin has a reduced affinity for oxygen in the presence of CO2. The greater the concentration of carbon dioxide, the more readily the hemoglobin releases its oxygen (the Bohr effect).

Case 1 at the gas exchange surface (lungs) Level of CO2 is low as it diffuses out across the exchange surface Affinity of hemoglobin for O2 is increased High concentration of O2 in the lungs Oxygen gets readily loaded by hemoglobin Reduced CO2 levels shift the curve to the left Case 2 in rapidly respiring tissues (muscles) Level of CO2 is high Affinity of hemoglobin for O2 is reduced Low concentration of O2 in the muscles Oxygen is readily unloaded from hemoglobin Increased CO2 levels shift the curve to the right More the concentration of CO2, the more readily hemoglobin releases its O2. This is because dissolved CO2 is acidic & low pH causes hemoglobin to change shape.

 At the gas exchange surface CO2 is expelled out concentration of CO2 is low pH is raised Higher pH changes hemoglobin to a shape that can load O2 easily Affinity of hemoglobin for O2 is increased In tissues, CO2 is produced by respiring cells high concentration of CO2 pH of the blood is lowered Lower pH changes hemoglobin to a shape that can unload O2 easily Affinity of hemoglobin for O2 is decreased The more active a tissue, the more oxygen is unloaded. Hemoglobin releases its O2 into respiring tissues Higher the rate of respiration More CO2 the tissues produce Lower the pH Greater the hemoglobin shape change More readily the O2 is unloaded the more O2 is available for respiration

Loading, transport & unloading of O2

 In humans, hemoglobin normally become saturated with oxygen as it passes through the lungs. Most of the hemoglobin molecules are loaded with their maximum four oxygen molecules. When this hemoglobin reaches a tissue with a low respiartory rate, only one of these molecules will normally be released. If a tissue is very active (an exercising muscle), then three oxygen molecules will usually be unloaded from each hemoglobin molecule.

Different Haemoglobins
Case 1: Lugworms live in the mud in estuaries and seashores. When the tide is out the lugworm stays in a burrow filled with sea water. But the oxygen concentration in this burrow can fall very low as the lugworm respires, so the lugworm has haemoglobin with a very high affinity for O2: its oxygen dissociation curve is shifted up. This allows the lugworm to obtain oxygen even when the PO2 is as low as 2kPa.

Case 2 : A human fetus makes a different kind of haemoglobin from an adult. Fetal haemoglobin has a higher affinity for oxygen at low partial pressures, so its oxygen dissociation curve is shifted up. A developing fetus obtains its oxygen, not through its lungs, but from its mothers blood in the placenta. So this different haemoglobin allows oxygen to diffuse from the mothers blood to the fetus, and to be unloaded in the fetal tissues. Fetal haemoglobin is gradually replaced by adult haemoglobin during the first year after birth.

Case 3 : Mice lose heat very quickly due to their large surface area to volume ratio, so they have a high metabolic rate to generate more heat. Their tissues therefore have a constant demand for oxygen for respiration. The oxygen dissociation curve for mouse haemoglobin is shifted down compared to humans, so plenty of oxygen is unloaded to all tissues all the time.