Haemoglobin and oxygen + Cardiovascular disease Flashcards
(61 cards)
What is haemoglobin?
Protein molecules with a quaternary structure
What is a haemoglobin made up of?
A quaternary structure in which all 4 polypeptides are linked together to form an almost spherical molecule
What is each polypeptide in haemoglobin associated with?
A haem group - contains ferrous (Fe2+ ion)
What can each ferrous ion in haemoglobin bind with?
One oxygen molecule, so one haemoglobin can carry 4 oxygen molecules in humans
What is the equation for the formation of oxyhemoglobin?
Hb + 4O2 = HbO8
What is the process by which haemoglobin binds with oxygen called?
Loading or associating
Happens in lungs
What is the process by which haemoglobin releases oxygen called?
Unloading or disassociating
Happens in tissues
To be efficient at transporting oxygen, what must haemoglobin do?
- Readily associate with oxygen at the surface where gas exchange takes place
- readily dissociate from oxygen at the tissues requiring it
What is the property of haemoglobin that makes it efficient?
It changes its affinity(chemical attraction) for oxygen under different conditions
How can haemoglobin change its affinity?
Its shape changes in the presence of certain substances e.g. co2
How does the shape of haemoglobin change in the presence of CO2?
The new shape binds more loosely to oxygen and so it releases it - has a lower affinity
Why are there different haemoglobin?
Each species produces a haemoglobin with a slightly different amino acid sequence and so different tertiary and quaternary structure and so different oxygen binding properties
What happens when haemoglobin is exposed to different partial pressures of oxygen?
It does not bind to oxygen evenly
What does the initial shape of the haemoglobin make it difficult to do?
For the first oxygen to bind to one of the sites on its 4 polypeptide units as they are closely united
What happens at low oxygen concentrations?
Little oxygen binds to haemoglobin (on oxygen dissociation curve, shallow gradient initially)
What happens to the shape of the haemoglobin after the 1st oxygen binds?
Quaternary structure changes, causing it to change shape
How does the change of the quaternary structure of haemoglobin after the binding of the 1st oxygen aid the binding of the other oxygens?
The binding of the first oxygen induces the other subunits to bind to an oxygen
What does the changing of the quaternary structure of the haemoglobin after the binding of the 1st oxygen mean?
It takes a smaller increase in partial pressure of oxygen to bind the 2nd oxygen than it did to bind the 1st one - known as positive cooperatively (gradient steepens)
What happens after the binding of the 3rd oxygen molecule to haemoglobin?
- Harder for 4th one to bind due to probability
- Majority of binding sites occupied
- Less likely that a single oxygen will find an empty site
- Gradient of curve reduces and flattens off
What is the affinity of haemoglobin like to the left of the curve?
Greater and vice versa
What is the Bohr effect?
The greater the concentration of CO2, the more readily haemoglobin releases oxygen
At the gas exchange-surface, what is the concentration of CO2 like?
Low
What happens given that the concentration of CO2 is low at the gas exchange surface?
- Affinity of haemoglobin for O2 increases
- High concentration of O2 in lungs
- Both ensure that O2 is readily loaded by haemoglobin
- Oxygen disassociation graph shifted to left
What is the concentration of CO2 like in rapidly respiring tissues?
High