Oxygen Transport and Oxygen Dissociation Curves

Oxygen Transport and Oxygen Dissociation Curves
Oxygen is not very soluble in blood, so the role of hemoglobin is to transport oxygen.
To be efficient at transporting oxygen, hemoglobin must:
• Readily associate/ load oxygen at the surface where gas exchange takes
place (lungs)
• Readily dissociate/ unload oxygen at respiring tissues requiring oxygen
Binding of oxygen to HB by cooperative binding:

The binding of successive oxygen atoms causes a conformational change that alters
the tertiary structure of the HB and makes binding easier.
The cooperative binding of oxygen gives the oxygen dissociation curve.
This curve shows the percentage of saturation of HB with O2 in relation to how much
O2 is available in the environment. Because of cooperative binding the curve shows
a sigmoidal shape. If binding was not cooperative, the dissociation curve would be a
straight line. This makes HB ideally suited to load O2 at lungs and unload in the
tissues.
1
• The shape of the haemoglobin molecule makes it difficult for the first oxygen
molecule to bind to one of the sites on its four polypeptide subunits because
they are closely united. Therefore, at low oxygen concentrations, little oxygen
binds to haemoglobin. The curve is shallow initially.
• However, due to cooperative binding, the binding of the first oxygen
molecule changes the quaternary structure of the Hb causing a
conformational change in its shape. This change makes it easier for other
subunits to bind to oxygen.
• At this stage, it takes a smaller increase in the partial pressure of oxygen to
bind more oxygen. The gradient of the curve steepens.
• The situation however changes after the binding of the third oxygen molecule.
With majority of oxygen binding sites are occupied, it is less likely for more
oxygen to bind, so the gradient of the curve is reduced, and the graph flattens
off.
As deoxygenated blood affects the lungs, a small increase in the partial pressure of
oxygen (pO2) causes a disproportionately large increase in the percentage saturation
of HB (the steep part of the curve). So HB has a high affinity for O2 when partial
pressure is high.
As the oxygen blood affects tissues, a small decrease in the pO2 causes a
disproportionately large decrease in the percentage saturation of HB. So HB has a
low affinity for O2 when the partial pressure is low.
2
Sigmoidal shape of the curve:
• Affinity of Hb for oxygen is low at low pO2

• Affinity of Hb for oxygen is high at high pO2.
Two rules for OXDC:
The further the curve is to the right, ①HB for oxygen affinity decreases, ②so
more oxygen is unloaded (released) to cells
The further the curve is to the left, ①HB for oxygen affinity increases, ②so
more oxygen is loaded to RBC
Carbon Affinity of
Region of Oxygen
dioxide haemoglobin for Result
body concentration
concentration oxygen
Oxygen is
Lungs High Low High associated/
loaded
Oxygen is
Respiring
Low High Low dissociated/
tissues
unloaded
3
Carbon Dioxide Transport in blood and Bohr Effect
Transport of CO2 in red blood cells (Role of RBC in carrying CO2)
1. Carbon dioxide diffuses into red blood cell

2. Where it combines with water (H2O + CO2 à H2CO3)
3. To form carbonic acid
4. This dissociates into hydrogencarbonate and proton (HCO3 à HCO3- +H+)
5. This reaction is catalyzed by carbonic anhydrase
6. Proton/ H+ combines/ buffered by haemoglobin
7. Forming haemoglobnic acid / HBB
8. Hydrogencarbonate (ions) diffuse into plasma out of red blood cell
9. Reference to chloride shift
10. Reference to attachment of carbon dioxide to haemoglobin
11. Forming carbaminohaemoglobin
12. Reference to carbon dioxide carried in solution in RBC
13. Reverse happens in alveoli/ CO2 diffuses into alveoli
Role of carbonic anhydrase:

1 catalyses the reaction in red blood cells, between carbon dioxide and water / to
form carbonic acid ;
2 (carbonic acid dissociates to form) hydrogencarbonate ions / bicarbonate
ions / HCO3– ;
3 very fast reaction ;
4 maintains (steep) concentration gradient for diffusion of carbon dioxide from
tissues to blood ;
5 catalyses reverse reaction in the lungs ;
6 hydrogencarbonate ions / bicarbonate ions / HCO3– , diffuse, into the plasma ;
4
Importance of Bohr Effect, why do we need the Bohr Effect/ shift?
• At lower pO2 (left of curve), % saturation of Hb decreases where Hb releases

more oxygen to muscle tissue (more dissociation of oxyhaemoglobin);
• An increase in carbon dioxide increases production of carbonic acid;
• which increases hydrogen ions in red blood cells (and reduces pH);
• Haemoglobin accepts hydrogen ions to form haemoglobinic acid as it has an
affinity to hydrogen ions
• This reduces affinity of Hb to oxygen, so more unloading to cells
Shift to the right and lower, means more oxyhaemoglobin is dissociated as PCO2 is
getting higher. More CO2 increases production of carbonic acid which increases
production of H+ ions. More H+ ions are accepted by HB forming HHb (higher
affinity for H+) so reduced affinity for oxygen.
1. At higher partial pressure of carbon dioxide, affinity of hameoglobin for

oxygen is reduced
2. Therefore, releases oxygen more readily, and percentage saturation with
oxygen falls (faster oxygen dissociation)
3. At the same partial pressure of oxygen
4. So oxygen is released to actively respiring or exercising tissues
Hemoglobin's affinity for oxygen increases with increasing pH and vice versa.
When CO2 builds up, this reduces the pH (due to carbonic acid formation), which
may cause a conformational change to the Hb and its affinity to oxygen is reduced
(so less oxygen loaded and more unloaded to cells).
5
Fetal HB= higher affinity to oxygen so more oxygen saturation at lower PO2.
After birth, adult HB (to the right) replaces the fetal HB.
Adult HB has a lower affinity for oxygen meaning that it would unload and release
oxygen more readily to respiring cells.
Explain how both fetal and adult Hb are adapted for their functions
The OXDC for fetal Hb is shifted to the left, so there is higher affinity of fetal Hb for oxygen
at lower partial pressure of oxygen, so fetal Hb can load more oxygen.
The OXDC of adult Hb is further to the right, so the adult Hb has a lower affinity of oxygen,
so it can unload more oxygen to respiring tissues.

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Oxygen Transport and Oxygen Dissociation Curves

Binding of oxygen to HB by cooperative binding:

The cooperative binding of oxygen gives the oxygen dissociation curve.

• Affinity of Hb for oxygen is low at low pO2

Two rules for OXDC:

Transport of CO2 in red blood cells (Role of RBC in carrying CO2)

1. Carbon dioxide diffuses into red blood cell

Role of carbonic anhydrase:

• At lower pO2 (left of curve), % saturation of Hb decreases where Hb releases

1. At higher partial pressure of carbon dioxide, affinity of hameoglobin for

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