OCR · A-Level · Biology
Course version: H420 · Version from Sept 2025
(i) the role of haemoglobin in transporting oxygen and carbon dioxide
Full specification wording
Transport in animals: (i) the role of haemoglobin in transporting oxygen and carbon dioxide
Haemoglobin is a quaternary protein with four haem groups, each containing an iron ion (Fe²⁺) that binds one oxygen molecule, so a fully loaded molecule carries four oxygen molecules.
Checked against the OCR H420 specification (opens in a new tab) on .
- Point 9 of 10
- 4 key terms
Study notes
From the checked teaching notes for this specification point.
The idea
Haemoglobin is a quaternary protein with four haem groups, each containing an iron ion (Fe²⁺) that binds one oxygen molecule, so a fully loaded molecule carries four oxygen molecules. In the lungs, a high partial pressure of oxygen (pO₂) causes oxygen to associate with haemoglobin, forming oxyhaemoglobin; in respiring tissues, a lower pO₂ causes oxygen to dissociate and be released. The affinity changes with pO₂, giving the S-shaped oxygen dissociation curve, and a high partial pressure of carbon dioxide lowers affinity further (the Bohr shift), increasing oxygen release where respiration is greatest. For carbon dioxide, most is transported as hydrogencarbonate ions (HCO₃⁻) formed in red blood cells by carbonic anhydrase, with some carried bound to haemoglobin as carbaminohaemoglobin and a small fraction dissolved in plasma.
What earns the marks
- States that haemoglobin has four haem groups, each with an iron ion (Fe²⁺) that binds one oxygen molecule, so four oxygen molecules are carried per molecule.
- Explains that oxygen associates with haemoglobin at high pO₂ in the lungs to form oxyhaemoglobin.
- Explains that oxygen dissociates from haemoglobin at lower pO₂ in respiring tissues and is released.
- Describes the S-shaped oxygen dissociation curve and the effect of a high pCO₂ lowering affinity (the Bohr shift).
- States that most carbon dioxide is transported as hydrogencarbonate ions (HCO₃⁻), formed with the enzyme carbonic anhydrase.
- States that some carbon dioxide is carried bound to haemoglobin as carbaminohaemoglobin and a small amount dissolves in plasma.
Common mistakes and how to put them right
Saying haemoglobin carries one oxygen molecule.
Put it right: Each of the four haem groups binds one oxygen molecule, so four are carried.
Claiming all carbon dioxide is carried as hydrogencarbonate.
Put it right: Some is bound to haemoglobin and a small fraction dissolves in plasma.
Reversing the Bohr shift.
Put it right: A high pCO₂ lowers haemoglobin's affinity for oxygen, increasing release in respiring tissues.
Exam tips
- Link each transport statement to the partial pressure conditions in lungs versus respiring tissues.
- Use the correct terms: association and dissociation for oxygen, and name the enzyme carbonic anhydrase for hydrogencarbonate formation.
- When describing the dissociation curve, refer to the S shape and explain the plateau and steep region in terms of affinity.
Try the lesson
The start of the Transport in animals: (i) the role of haemoglobin in transporting oxygen and carbon dioxide lesson, made from checked teaching notes for this specification point.
Have a go first
In which region of a haemoglobin molecule does oxygen bind?
Listen
Haemoglobin is a quaternary protein with four haem groups, each containing an iron ion (Fe²⁺) that binds one oxygen molecule, so a fully loaded molecule carries four oxygen molecules. In the lungs, a high partial pressure of oxygen (pO₂) causes oxygen to associate with haemoglobin, forming oxyhaemoglobin; in respiring tissues, a lower pO₂ causes oxygen to dissociate and be released. The affinity changes with pO₂, giving the S-shaped oxygen dissociation curve, and a high partial pressure of carbon dioxide lowers affinity further (the Bohr shift), increasing oxygen release where respiration is greatest. For carbon dioxide, most is transported as hydrogencarbonate ions (HCO₃⁻) formed in red blood cells by carbonic anhydrase, with some carried bound to haemoglobin as carbaminohaemoglobin and a small fraction dissolved in plasma. A strong answer earns marks for these points. States that haemoglobin has four haem groups, each with an iron ion (Fe²⁺) that binds one oxygen molecule, so four oxygen molecules are carried per molecule. Explains that oxygen associates with haemoglobin at high pO₂ in the lungs to form oxyhaemoglobin. Explains that oxygen dissociates from haemoglobin at lower pO₂ in respiring tissues and is released. Describes the S-shaped oxygen dissociation curve and the effect of a high pCO₂ lowering affinity (the Bohr shift). Exam tip: Link each transport statement to the partial pressure conditions in lungs versus respiring tissues.
See it
Key words
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Structure of haemoglobin and oxygen binding
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Association and dissociation of oxygen
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Oxygen dissociation curve and the Bohr shift
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Carbon dioxide transport forms
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See every definition
- Structure of haemoglobin and oxygen binding
- A quaternary protein with four haem groups, each containing an iron ion (Fe²⁺) that binds one oxygen molecule, so a fully loaded molecule carries four oxygen molecules.
- Association and dissociation of oxygen
- At high pO₂ in the lungs oxygen associates with haemoglobin to form oxyhaemoglobin, while at lower pO₂ in respiring tissues oxygen dissociates and is released.
- Oxygen dissociation curve and the Bohr shift
- Affinity changes with pO₂ to give the S-shaped oxygen dissociation curve, and a high pCO₂ lowers affinity further, increasing oxygen release where respiration is greatest.
- Carbon dioxide transport forms
- Most is transported as hydrogencarbonate ions (HCO₃⁻) formed in red blood cells by carbonic anhydrase, some is bound to haemoglobin as carbaminohaemoglobin and a small fraction dissolves in plasma.
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