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Red blood cells (also called erythrocytes) are specially adapted to carry gases around the body. When they mature, they lose their nucleus and mitochondria. This frees up space for a large amount of the protein haemoglobin, which is the main gas-carrying molecule.
Each mature RBC also contains the enzyme carbonic anhydrase, which is essential for carbon dioxide transport (explained below).
Haemoglobin (Hb) is a large protein made of four subunits — two alpha (α) chains and two beta (β) chains. Each subunit contains a haem group, which is a special region with an iron ion (Fe²⁺) at its centre. This iron ion is where one oxygen molecule (O₂) binds.
Because there are four haem groups in total, one haemoglobin molecule can carry four oxygen molecules at once.
When oxygen binds to haemoglobin, it forms oxyhaemoglobin:
Hb + 4O₂ ⇌ HbO₈ (oxyhaemoglobin)
This reaction is reversible — haemoglobin picks up oxygen in the lungs and releases it in the tissues. The binding of oxygen is also cooperative: when the first oxygen molecule binds, the haemoglobin changes shape slightly (called an allosteric change), making it easier for the next three oxygen molecules to bind. This is known as co-operative binding.
About 95–97% of oxygen in the blood is carried as oxyhaemoglobin. The remaining 3–5% is simply dissolved in the plasma.
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