Biology Chapter 7 Flashcards
(146 cards)
Describe the quaternary structure of haemoglobin
4 polypeptides linked together: 2 alpha and 2 beta groups. 4 ferrous ions, one bound to each polypeptide, which can each bind to one oxygen molecule
How many oxygen molecules can be carried by one haemoglobin molecule?
4
Name 2 properties of haemoglobin which can make it efficient at transporting oxygen
Readily associates with oxygen when oxygen is plentiful
Readily releases oxygen where oxygen is needed
How does haemoglobin achieve efficiency at transporting oxygen
It changes its affinity for oxygen according to conditions. Its shape changes in high carbon dioxide to release oxygen
How does carbon dioxide concentration affect whether haemoglobin is released or attached?
Low carbon dioxide concentration = oxygen is attached
High carbon dioxide concentration = oxygen is released
Suggest why the concentration of oxygen is low in respiring tissues, while the concentration of carbon dioxide is high
Because oxygen is being used up to produce energy, and carbon dioxide is a by-product of respiration
Define ‘high affinity’
Easily takes up oxygen but gives it away less readily
Define ‘low affinity’
Releases oxygen more readily but takes up oxygen less readily
Explain how the environment can influence the type of haemoglobin an organism exhibits
When little oxygen is available from the environment, haemoglobin must be able to bind as much of it as possible
Explain how metabolic rate can influence the type of haemoglobin an organism exhibits
A high metabolic rate means the organism needs oxygen readily available; therefore, it needs a type of haemoglobin that can release oxygen readily
Why do different haemoglobins have different affinities for oxygen?
Slightly different amino acid sequences means that haemoglobins have different shapes and affinities
Define ‘loading/associating’
Haemoglobin combining with oxygen
Define ‘unloading/dissociating’
Oxygen being released from haemoglobin
Why, at very low concentrations of oxygen, is it difficult for haemoglobin to load the first oxygen molecule?
There is a close union between the 4 polypeptides of the haemoglobin molecule
What is meant by ‘partial pressure’?
The proportion of the total pressure that is contributed by a particular gas in a mixture
What is measured on the x-axis of an oxygen dissociation curve?
Partial pressure of oxygen (KPa)
What is measured on the y-axis?
Saturation of haemoglobin with oxygen (%)
Why does the graph show a steep rise in oxygen saturation of haemoglobin at higher concentrations of oxygen?
After the first oxygen molecule has bound, it is much easier for the other 3 polypeptides to binds to oxygen
What is the name given to the graph of the relationship between oxygen binding and oxygen concentration?
Oxygen dissociation curve
Explain why the graph tails off at high concentrations of oxygen
The haemoglobin molecule is saturated
How are the oxygen dissociation curves of different haemoglobins similar?
Similar S-shaped curves
How are oxygen dissociation curves different?
Different positions on the axes
The further to the left the curve…
the greater the affinity for oxygen
The further to the right the curve…
the lower the affinity for oxygen