Transcript Haemoglobin Presenta..

Haemoglobin
Basic Knowledge:
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Haemoglobin is an iron protein - compound in red blood cells that transports
oxygen, carbon dioxide, and nitric oxide.
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It carries oxygen to body cells. After releasing oxygen to the body tissues,
haemoglobin picks up carbon dioxide and transports it to the lungs.
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Haemoglobin is contained entirely in the red blood cells.
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A lack of haemoglobin caused by iron deficiency leads to anaemia .
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Haemoglobin containing iron is the reason for the red colour of blood:
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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.
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This comes in handy for oxygen transport!
Haemoglobin: the Protein
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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
Haemoglobin: the Protein
Structure:
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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.
Haemoglobin’s Structure:
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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.
Haemoglobin: the Oxygen Carrier
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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.
How Does It Do It?
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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.
Haemoglobin Variations:
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Myoglobin.
Myoglobin is the muscle’s 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.)
Foetal Haemoglobin
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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.
Anaemia:
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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.
Ye Olde End
Mastermind, genius and director:
Charlie Wilkes
Helpful Person / Researcher: James Johnson
Slacker: Roshan Tajapra.