Haemoglobin

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Haemoglobin
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Basic Knowledge

• Haemoglobin is an iron protein - compound in red
  blood cells that transports oxygen, carbon
  dioxide, and nitric oxide.
• It carries oxygen to body cells. After releasing
  oxygen to the body tissues, haemoglobin picks up
  carbon dioxide and transports it to the lungs.
• Haemoglobin is contained entirely in the red
  blood cells.
• A lack of haemoglobin caused by iron deficiency
  leads to anaemia .
• Haemoglobin containing iron is the reason for the
  red colour of blood
• Iron has a variable oxidation state, where it can
  form more than one stable ion with its outermost
  electron in the d-orbital it is a transition
  metal.
• This comes in handy for oxygen transport!

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Haemoglobin the Protein

• Human haemoglobin consists of four chains
• Two identical Alpha chains
• And two identical Beta chains.
• Each of these chains is bound to a non protein
  group called haem. This results in

Haemoglobin
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Haemoglobin the Protein
Structure

• Haemoglobin has a primary, secondary, tertiary
  and quaternary structure
• Secondary alpha helix.
• Tertiary helical and non - helical units fold to
  form a compact unit.
• Quaternary when all four separate chains group
  to form the full protein.
• The quaternary structure is what makes each
  protein so very individual.

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Haemoglobins Structure

• The diagram to the right is how the four protein
  chains pack together to form human haemoglobin
• Green and yellow alpha.
• Blue and orange beta.

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Haemoglobin the Oxygen Carrier

• Haemoglobin is responsible for oxygen transport.
• Haemoglobin contains Iron (II) ions Fe2
• Iron has a variable oxidation state, so oxygen
  can bind to it this is where blood changes
  colour!
• Because each haemoglobin molecule has four haem
  groups, it can bond to four oxygen molecules.

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How Does It Do It?

• Oxygen binds easily to haemoglobin.
• When it is needed (for example in muscles),
  oxygen is released.
• There is an enzyme in red blood cells cytoplasm
  called carbonic anhydrase.
• This prompts CO2 and H2O to bind together to form
  H2CO3.
• H ions are formed, which then bond to
  haemoglobin to form HHb Haemoglobinic acid.
• This bond then displaces the oxygen, which is
  released.

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Haemoglobin Variations

• Myoglobin.
• Myoglobin is the muscles version of haemoglobin.
• It has a much deeper red colour.
• It can only accept two oxygen molecules.
• It only releases oxygen in times of EXTREME need.
  (Like exercise.)

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Foetal Haemoglobin

• Foetuses do not acquire their oxygen through
  their lungs.
• Oxygen is diffused across the placenta.
• Foetal Haemoglobin has a higher affinity for
  oxygen than maternal haemoglobin.
• This allows it to attract oxygen from the
  mother to use for aerobic respiration.

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Anaemia

• This is when one of the four chains in
  haemoglobin contains one different amino acid
  than normal.
• This results in the red blood cell forming a
  sickle shape thus it is called
• Sickle Cell Anaemia.
• Normally caused by a lack of iron, but some types
  are genetic.

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