Session 10: Protein Function and Oxygen Transport Flashcards
What two molecules are responsible for the transport of oxygen in the body?
Haemoglobin
Myoglobin
Apart from oxygen, Haemoglobin also transports what?
CO2 and protons
What is the role of myoglobin?
To act as a small oxygen reservoir in MUSCLE
Why is it necessary that oxygen is carried by transporters in the body?
Oxygen is not very water soluble
Describe the structure of haem
Haem consists of:
A protoporphyrin ring
A Fe atom
Four Nitrogen atoms
What is the function of the haem group?
To bind oxygen
Myoglobin is made up of how many polypeptide chains?
One
How many molecules of oxygen can bind to the haem group(s) of haemoglobin and myoglobin?
One oxygen molecule
How may haem groups are there per polypeptide chain in haemoglobin and myoglobin?
One
How does the Fe (Iron) atom bind to the haem protein and hold it in the ring?
Proximal histidine
Myoglobin is made up by 75% of what secondary protein structure?
alpha-helix
The alpha-helix is myoglobin is covalently linked to what? Where does it make this link?
Histidine residue
In the 8th alpha-helix
Where does the Fe (Iron) sit in DEOXYmyoglobin?
Slightly below the plane of the ring
In deoxymyoglobin, what happens to the Fe when oxygen binds?
It moves up into the plane of the ring which causes movement of the histidine residue and a change in the overall conformation of myoglobin
What shape is the oxygen binding curve for myoglobin?
Hyperbolic curve
What is p50 and what is its constant value in myoglobin?
The partial pressure of oxygen at which the saturation of oxygen binding to myoglobin is 50%
2 torr
What shape is the oxygen binding curve for haemoglobin?
Sigmoidal curve
Describe the structure of haemoglobin
4 polypeptide chains
A haem group attached to each polypeptide chain, each with the capability of binding an oxygen
What is important for defining the sigmoidal shape of haemoglobin’s oxygen binding curve?
The entire molecular structure and how it can change to give high and low affinity states
Haemoglobin exists in two states relative to its binding affinity. What are they?
R state “relaxed” - High affinity for oxygen
T state “tense” - Low affinity for oxygen
Describe the differences in the structure between the R and T state and how this relates to haemoglobin’s affinity for oxygen
T state: The haem groups are not exposed and the structure is stabilised by interactions between histidine (+) and aspartate (-) residues–> LOW AFFINITY
R state: Is rotated around 15 degrees which means the interactions can no longer be made and the haem groups are exposed for oxygen to bind to –>HIGH AFFINITY
The binding of oxygen promotes the formation of which of the two states of haemoglobin?
R state (high affinity)