Haemoglobin

• Haemoglobin is a group of polypeptides in a quaternary structure that transport oxygen using Fe2+ haems
• Oxygen is loaded onto haemoglobin in high partial pressures of oxygen regions (alveoli) and unloaded in low partial pressures of oxygen regions (respiring cells), shown by the dissociation curve
• Cooperative binding is when the original oxygen binds causing a change in shape on haemoglobin, causing more to bind
• Bohr Effect is when high concentrations of CO2 causes the oxyhaemoglobin curve to shift to the right, the affinity of oxygen decreases as the acidic climate changes haemoglobins tertiary structure
• A low partial pressure of CO2 in the alveoli due to expiration cause an increased affinity of oxygen
• A high partial pressure of CO2 in respiring tissues due to CO2 production cause affinity of oxygen to decrease, unloading oxygen there
• Myoglobin is foetal haemoglobin, with a higher affinity for oxygen even at the same partial pressures as an adult, allowing offloading to babies haemoglobin from mothers on the placenta walls
• Llamas are specialised due to higher altitudes, they have a higher affinity of oxygen due to lack of oxygen higher up
• Doves are specialised to have a lower affinity of oxygen due to faster metabolisms, they can more readily unload oxygen for respiration