8.3 Haemoglobin Flashcards
composition
2 alpha polypeptide chains
2 beta polypeptide chains
each chain has a prosthetic haem group attached to it
arrangement of polypeptide chains
hydrophobic R groups facing inwards; hydrophilic R groups facing outwards
why can Hb bind with O2?
presence of Fe2+ in Haem group
reaction between Hb & O2
Hb + 4O2 –> HbO8
reversible reaction
benefit of being soluble
can dissolve in blood plasma; transported easily
benefit of having small surface area: volume ratio
can be transported in large concentrations through narrow vessels
cooperative binding: meaning
every time a polypeptide chain binds with O2 the molecule undergoes a conformational change that makes subsequent binding easier
cooperative binding: impact
Hb has a high affinity for binding with O2
why does Hb unload O2 in the muscles? (3)
- low pO2; oxygen diffuses into tissue cells
- protons compete with O2 for Hb
- CO2 competes with O2 for Hb
reaction for formation of carbonic acid
CO2 + H2O –> H2CO3
disassociation of carbonic acid
H2CO3 –> H+ + HCO3-
reversible reaction
reaction for protons binding with haemoglobin
HbO2 + H+ –> H+Hb + O2
reversible reaction
reaction for CO2 binding w Hb
CO2 + HbO2 –> Hb-COO- + O2 + H+
what happens to hydrogencarbonate after carbonic acid disassociates?
it moves out of the RBC and into the blood plasma
name of molecule formed after Hb and CO2 bind
carbaminohaemoglobin