1.2 haemoglobin Flashcards
structure of haemoglobin 1
Has quaternary structure AND is conjugated (protein with an non protein group).
structure of haemoglobin 2
it is made up of 4 connected polypeptide subunits linked by bonds between R groups of the polypeptide chains.
structure of haemoglobin 3
Each subunit has prosthetic group (non-protein group) called haem it is tightly bound to the protein is essential for its function (iron in haemoglobin is the binding site of oxygen)
chain effect
Each haem group can bind one oxygen molecule
- Binding of one oxygen molecule increases affinity of remaining haem groups for Oxygen
conformational change
Caused by conformational change to protein when each oxygen binds which increases the affinity of the remaining subunits for o2 the same is true in reverse
effect of PH and temp
Decreased pH decreases affinity (respiring tissue produces more co2 which is acidic) / increased pH increases affinity
- Decreased temp increases affinity (respiring tissue such as muscles rises heat) / increased temp decreases affinity
PH effect named
Decreased affinity caused by decreased pH is known as the Bohr effect.