topic 4.5 - transport of gases in the blood Flashcards
what is the main job of haemoglobin
to transport oxygen around the body
transport of oxygen - how do the molecules bind?
- 1st oxygen molecule that binds alters the arrangement of the molecule
- easier for the following oxygen molecules to bind
- final O2 molecule binds a lot faster than first
- same process in reverse when oxygen dissociates from haemoglobin
structure of haemoglobin and how it transports oxygen
- haemoglobin is a large globular protein
- made up of 4 peptide chains, each with an iron containing prosthetic group (haem group)
- can pick up 4 molecules of O2 in a reversible reaction to form oxyhaemoglobin
Hb + 4O2 ⇌ Hb4O2
haemoglobin + oxygen ⇌ oxyhaemoglobin
transport of oxygen - how do the molecules bind? (positive cooperativty)
- 1st oxygen molecule that binds to iron alters the arrangement of the haemoglobin molecule
- easier for the following oxygen molecules to bind
- final O2 molecule binds a lot faster than first
- same process in reverse when oxygen dissociates from haemoglobin
where is the partial pressure of oxygen high
- the lungs have a high pp of oxygen
- so oxygen binds rapidly with haemoglobin to form oxyhaemoglobin
why does the percentage saturation of oxygen in the lungs not reach 100%
- most iron atoms are already bound to the oxygen molecules
- the probability of a collision between an unbound iron atom and oxygen molecule is low
oxygen levels in body tissues
- relatively low
- concentration of oxygen in cytoplasm of RBC is higher than in the surrounding tissue
- hence, O2 moves out by diffusion down its concentration gradient
- haemoglobin gives up some of its O2
Bohr effect
- in the presence of CO2 the affinity of haemoglobin for oxygen decreases so it is released
- hence, oxygen dissociates from haemoglobin and can be used in respiring tissues
- changes in carbon dioxide concentration result in changes in the curve - Bohr effect
Bohr effect - haemoglobin and oxyhaemoglobin dissociation curve - increased CO2
- increase in CO2 causes curve to shift to the right
- oxygen associates less readily and dissociates more readily
Bohr effect - haemoglobin and oxyhaemoglobin dissociation curve - decreased CO2
- decrease in CO2 causes curve to shift to the left
- oxygen associates more readily and dissociates less readily
what happens when oxygen dissociates from haemoglobin?
- gets harder to remove the oxygen
- conc of oxygen in RBC when blood enters is low
- concentration of oxygen in cytoplasm of RBC is higher than in surrounding tissue
- hence oxygen moves into cells via diffusion down its concentration gradient
what is myoglobin
- respiratory pigment found in muscle tissue of vertebrates
- small bright red protein
structure of myoglobin and how this relates to its function
- similar to a single haemoglobin chain
- single polypeptide chain
- contains haem group which binds oxygen
- has a higher affinity for oxygen so becomes easily saturated
- once bound to oxygen, it doesn’t give up oxygen easily hence acts as an oxygen store
similarities between haemoglobin and myoglobin
- both globular proteins
- both contain haem group/s
differences between haemoglobin and myoglobin
- higher oxygen affinity in Mb
- haemoglobin carries oxygen to cells in body whereas Mb stores oxygen in muscle cells to be used as energy
- Hb has quarternary structure, Mb has tertiary structure
- higher conc of Hb in blood, higher conc of Mb in heart & muscle cells