The oxygen dissociation curve shows the relationship between the partial pressure of oxygen in the environment and the percentage saturation of haemoglobin with oxygen.At low oxygen concentrations, little oxygen is bound to haemoglobin because the subunits are closely bound and in close proximity making it difficult for the first oxygen molecule to bind.The binding of the second molecules is easier due to the change in the shape of the haemoglobin molecule when the first oxygen molecule binds. It takes a smaller increase in partial pressure to bind the second molecule so the gradient of the curve is steeper.Binding of the third molecule is made easier by the binding of the second molecule. The subsequent ease of binding of one molecule due to the binding of another molecule by the change in shape is called positive cooperativity.With most of the binding site occupied the probability of the fourth molecule finding an empty binding site is low so the graph flattens.The further to the left the curve, the greater the affinity of haemoglobin for oxygen.
Oxygen Dissociation Curve
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Specification: AQA Biology (7401), AS-level, 3.3.4.1 Mass transport in animals. Topic: Mass Transport in Animals.
Key terms in this lesson
- haemoglobin
- A globular, quaternary protein in red blood cells, made of four polypeptide chains each with a haem group, that binds and transports oxygen.
More in Mass Transport in Animals
- Haemoglobin
- Loading and Unloading Oxygen
- Different Types of Haemoglobin
- Effect of Carbon Dioxide
- Transport of Oxygen
- Lugworm
- Llama
- Fetal Haemoglobin
All 27 lessons in Mass Transport in Animals · All AQA AS-level Biology topics