Haemoglobin

Question 1

Where is it found

Answer 1

Red blood cells(erythrocytes)

Question 2

structure of haemoglobin

Answer 2

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.

Question 3

How does haemoglobin load and unload oxygen

Answer 3

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.

Question 4

Bhor effect

Answer 4

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

Question 5

Importance of ion

Answer 5

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