haemoglobin Flashcards
why is oxygen needed by all living cells?
all living cells respire
equation for respiration
glucose + oxygen –> carbon dioxide + water + energy (ATP)
function of red blood cells?
contains haemoglobin which binds with oxygen to deliver cells
structure of haemoglobin?
each poly peptides contains a..?
quaternary structure - made up of 4 polypeptide chains - each of the polypeptides contains a heam group
what does each heam group contain?
this is the part of Haemoglobin that..?
Fe2+ (iron) ions
going to binds to oxygen
what is formed when haemoglobin binds with oxygen? what type of reaction is this?
oxyhaemoglobin
reversible reaction
oxygen + haemoglobin ⇌ oxyhaemoglobin
when oxygen unloads
lungs have a …? concentration of oxygen
High
tissues have a …? concentration of oxygen
Low
why does haemoglobin have ahigh affinity for oxygen in the lungs?
in the lungs at the alveoli, oxygen has entered the capillaries and it’s going to load on haemoglobin because of the high concentration/partial pressures of oxygen
in tissues oxygen is being used for?
respiration
why does the tissues have a low affinity for oxygen?
because of the low concentration of ocygen (being used up respiring tissues) so oxygen unloads from haemoglobin for respiring tissues
what are 4 key phrases associated with the Oxyhaemoglobin dissociation curve?
- Affinity of Hb to Oxygen - the ability of Hb to attract/bind to oxygen
- saturation of Hb with oxygen - when Hb is holding the maximum amount of oxygen it can bind
- loading/association of Hb - the binding of oxygen to Hb
- Unloading/ dissociation of Hb - when oxygen detaches/unbinds from Hb
draw an oxyhaemoglobin disassociation curve
what is the shape of the curve
s shape - sigmoid curve
describe the graph
- at low partial pressure of oxygen, as we increase the oxygen, the percentage saturation of oxygen doesnt increase that much.
- but once we get a little higher, the percentage saturation of oxygen increases readily for a small increase in oxygen
why is the graph S shaped?
- due to cooperative nature of oxygen binding. after the first oxygen molecule binds, shape of Haemoglobin changes, making it more easier for the 2nd haemoglobin then when this one binds it makes it easier for 3rd then 4th
- meaning that oxygen has a higher affinity for oxygen so on the graph the gradient get’s steeper
- the rate of increase in percentage saturation increases, as the oxygen further increases but after haemoglobin gets more saturated, it get’s harder for further molecules to bind and this is why it plateaus
what is the Bohr shift?
when we increase carbon dioxide in our blood e.g when we are excercising, we lower the pH pf the blood, so reduces the affinity for oxygen, because HB changes shape, making it harder for molecules to bind
explain why the Bohr shift is beneficial?
increases the amount of oxygen that’s being unloaded from haemoglobin at the tissues so the oxygen can be used for respiration
explain how the curve shifts in less acidic conditions?
- low partial pressure of CO2 in the alveoli
- curve shifts left
- increased affinity for oxygen so loads more oxygen
explain how the curve shifts in more acidic conditions?
- high partial pressure of carbon dioxide at respiring tissues
- curve shifts right
- decreased affinity for oxygen and unloads more oxygen
why is haemoglobin different in different organisms?
haemoglobins is a protein made up of amino acids, so if we change the sequence of amino acids, haemoglobin structure changes and so changes the affinity is has for oxygen
structure of haemoglobin differs depending on..?
the environment that the organism is adapted to live in
when curve has shifted to the left, what does this mean?
- heamoglobin has a higher affinity for oxygen, means that it loads more readily in the lungs at a low partial pressures of oxygen
this is useful for organisms living at..?
high altitudes - so low oxygen concentration- can load more oxygen into lungs
explain how foetal haemoglobin is adapted?
- has a higher affinity for oxygen than in adult haemoglobin
- this is important as by the time the mothers blood reaches the placenta, if oxygen saturation decreased because some has been used up for the mother body
- therefore foetal haemoglobin needs to be better at absorbing oxygen than the mothers heamoglobin so the foetus can still get oxygen from its mothers blood across the placenta
if in an organism the curve has shifted to the right..?
- they have alower affinity for oxygen
- so this is beneficial for our tissues
- at the same partial pressure of oxygen in the tissues, haemoglobin has a lower saturation for oxygen, this means that more oxygen has been unloaded into respiring tissues.
this would occur in organisms with..?
a high metabolic rate -> small, active organism
what does this do?
enables organism to survive better in their environments
what is myoglobin able to do?
another type of haemoglobin in muscle tissue in vertebrates which is able to store and hold onto oxygen even at very low partial pressures of oxygen
when partial pressures of myoglobin fall to very low levels, myoglobin…?
releases all of the oxygen it’s carrying
FINISH