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AQA Biology Haemoglobin
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AQA Biology Unit 2 Haemoglobin Chapter 4
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biology
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Resource summary
AQA Biology Haemoglobin
Structure
4 sub-units
Each sub-unit contains a protein chain (globin) and a haem group (prosthetic).
The haem group contain ferrous ions (Fe 2+)
Protein with a quaternary structure
Role of Hb
Oxygen can bind to haemoglobin in the lungs and be transported round the body in the blood
Oxygen can dissociate with haemoglobin at respiring tissue muscle when in limited supply
Partial Pressure
Oxygen concentration is expressed as partial pressure (kilopascals)
The percentage of Hb associated with Hb at a given partial pressure is called percentage saturation
Affinity
The degree to which Hb binds with oxygen
A high partial pressure (e.g in lungs) means there is a higher affinity for oxygen
Oxygen is therefore readily taken up
A low partial pressure (e.g in respiring tissue) the affinity for oxygen is low
Oxygen is therefore readily released
Bohr Effect/Shift
In the presence of CO2, the affinity for oxygen is lower
Oxygen is readily released when there is a high concentration of CO2
In lungs - low conc. of CO2 - increased affinity for O2 - promotes loading
In respiring tissue - high conc. of CO2 - decreased affinity for O2 - promotes unloading
Increased CO2 level causes the curve to shift the right
Oxygen Dissociation Curves
0 p O2 - no oxygen bound to Hb
At low p O2 - polypeptide chain is tightly packed - harder for oxygen to bind to iron ions - curve rises gently
As one molecule of O2 binds to one haem group, polypeptide chain opens up - other 3 groups exposed - easy for oxygen to bind - curve rises steeply
High p O2 - Hb becomes saturated - curve plateaus
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