Haemoglobin is a protein that binds oxygen when there is lots of oxygen available and releases oxygen when there is a low partial pressure of oxygen.Many different organisms have different haemoglobins which differ in structure and their affinity for oxygen.Haemoglobin has a quaternary structure. It is made of four polypeptide chains. Two alpha chains and two beta chains are held together by hydrogen bonds and other weak interactions to form a globular molecule. Haemoglobin also has a non-protein haem prosthetic group attached to each polypeptide chain. The haem prosthetic group contains iron, Fe2+, which binds oxygen.
Haemoglobin
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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
- quaternary structure
- The structure formed when two or more polypeptide chains, and sometimes a non-protein prosthetic group, are held together to form a functional protein.
- disulfide bridge
- A strong covalent bond formed between two sulfhydryl (-SH) groups of cysteine residues in a polypeptide.
More in Mass Transport in Animals
- Loading and Unloading Oxygen
- Different Types of Haemoglobin
- Oxygen Dissociation Curve
- 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