Oxygen Dissociation

Curves
Lecture 5

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:

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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).
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Effect of CO2 Concentration

Hemoglobin has a reduced affinity for oxygen in the presence of CO 2.
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 O 2 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 O 2 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 CO 2, the more readily hemoglobin
releases its O2. This is because dissolved CO 2 is acidic & low pH
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causes hemoglobin to change
shape.

Loading, transport & unloading of O2

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 O 2 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
Hemoglobin releases its O2 into respiring tissues

The more active a tissue, the more oxygen is unloaded.

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

 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.

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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.

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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.

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