2.3.5

Haemoglobin

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Haemoglobin

Haemoglobin is a globular protein found in red blood cells. Haemoglobin carries oxygen from the lungs around the body.

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Quaternary stucture

  • Haemoglobin is a protein made from four different polypeptide chains.
  • The four chains give haemoglobin a quaternary structure.
  • There are two alpha and two beta chains.
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Haem groups

  • Each polypeptide chain in a haemoglobin molecule has a haem group.
  • A haem group is a prosthetic group that is attached to the protein.
  • The haem groups contain an iron ion.
  • The iron ion is what makes haemoglobin red.
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Affinity

  • Haemoglobin has a high affinity (attraction) for oxygen.
  • When red blood cells reach the lungs, oxygen diffuses into the red blood cells and binds to haemoglobin.
  • Four molecules of oxygen bind to one molecule of haemoglobin.
  • When oxygen binds to haemoglobin, oxyhaemoglobin is formed.
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Dissociation

  • When the red blood cells reach the tissues in the body (e.g. muscle cells), oxygen is released from the oxyhaemoglobin in a process called dissociation.

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1Cell Structure

2Biological Molecules

3Enzymes

4Cell Membranes & Transport

5The Mitotic Cell Cycle

6Nucleic Acids & Protein Synthesis

7Transport in Plants

8Transport in Mammals

9Gas Exchange

10Infectious Diseases

11Immunity

12Energy & Respiration (A2 Only)

13Photosynthesis (A2 Only)

14Homeostasis (A2 Only)

15Control & Coordination (A2 Only)

16Inherited Change (A2 Only)

17Selection & Evolution (A2 Only)

18Classification & Conservation (A2 Only)

19Genetic Technology (A2 Only)

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