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Summary AQA ALEVEL BIOLOGY NOTES ON HAEMOGLOBIN £7.49   Add to cart

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Summary AQA ALEVEL BIOLOGY NOTES ON HAEMOGLOBIN

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ALEVEL NOTES ON HAEMOGLOBIN ADJUSTED TO THE AQA SPECIFICATION AND MADE FROM MARKSCHEMES

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  • July 2, 2023
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Haemoglobin

Haemoglobin 's role is to
transport oxygen
.




Haemoglobin has four Each
polypeptide


a
quaternary structure ,
in which all
polypeptide chains are linked together .
is

> + "
associated with haem Fe Each Fe combine with molecule
a
group ,
which contains a ion . ion can a
single oxygen

total of four single
( Oz ) ,
making a 0, molecules that can be carried by a haemoglobin .




form
In oxygen joins blood
in
the lungs to
haemoglobin red cells to
haemoglobin


•✗
.
,




turns back
Near the
body cells ,
oxygen leaves haemoglobin and it to
haemoglobin
-

☐✗ .




loading ( associating)
Hb 402 Hbos
'
+ ,


haemoglobin oxygen unloading oxy haemoglobin
(
dissociating)



Affinity of
Haemoglobin

for

Affinity oxygen means the tendency a molecule has to bind with



oxygen .




Haemoglobin changes its
affinity for under different conditions This is because its
shape changes in the





oxygen
.




of certain substances C02
presence ,
such as .




At of of
-



higher concentrations carbon dioxide , the new shape the
haemoglobin molecule binds more
loosely to

to hence
oxygen haemoglobin releases its
oxygen .




Region of Affinity of Result
po , poo ,
body haemoglobin for 02

Gas
exchange High Low High oxygen is

surface associated



Respiring ↳W High
Low oxygen is

tissues dissociated




Different Have Different Haemoglobin
Organisms

Each different
produces haemoglobin with
slightly primary hence different
tertiary &





species a a structure
quaternary
structure
leading to different
oxygen binding properties .




Depending its structure haemoglobin molecules from those that have high affinity for to those
-

on
range a
oxygen
for
that have a low
affinity oxygen .




Oxygen Dissociation Curves %
' " """"" " " " H e r r m a n n,
'
- , , , -
¥ ,




3
-
An dissociation curve shows how saturated the
oxygen
haemoglobin is with
oxygen at
any given partial pressure .




2
1 When
P02 is low ( At tissues )


-

At low concentrations little to
oxygen ,
oxygen binds

unloads
haemoglobin .

oxygen

Shape of the haemoglobin molecule makes it difficult for the
'



the first oxygen moecule to bind to one of the sites on its


four
polypeptide subunits because
they are
closely United .

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