Haemoglobin Flashcards
Where is it found
Red blood cells(erythrocytes)
structure of haemoglobin
It is a quaternary structured protein as it is made of 4 polypeptide chains . Each polypeptide chain contains a haem group containing iron ion which combines to oxygen.
How does haemoglobin load and unload oxygen
Haemoglobin can carry 4 oxygen molecules one at each haem group. In the lungs , at a high partial pressure haemoglobin has a high affinity for oxygen and as a result it readily associates with haemoglobin. At respiring tissues at a low partial pressure oxygen dissociates from haemoglobin.
Bhor effect
As concentration of CO2 is high the rate of unloading is faster. This is advantageous as it provides more oxygen for respiring tissue that are undergoing aerobic respiration
Importance of ion
Iron ion—> allows oxygen molecule to bind to haem group
no iron ion = haemoglobin function less efficiently as oxygen wont be loaded into haemoglobin ——-> no oxygen for respiring tissue and muscles.
Knock on effect on mitochondria as they need oxygen to produce ATP through oxidative phosphorylation