Haemoglobin Flashcards
What type of protein is haemoglobin
Globular
Why is it good that red blood cells do not contain a nucleus
Provides more space inside the cell for haemoglobin so that they can transport as much O2 as possible
What structure does haemoglobin have
Quaternary made up of 4 polypeptide chains
Describe the globin proteins in a haemoglobin
Four globin subunits are held together by disulphide bonds
Arranges so their hyrophobic R groups are facing inwards helping to preserve the three dimensional spheric shape
The hydrophilic R groups face outwards to maintain solubility
What does the haem group contain
Fe2+ which is able to reversibly combine with an oxygen molecules to form oxyhaemoglobin
How many oxygen molecules can be carried in a haemoglobin
Because of their four haem mgroups they can carry four oxygen molecules or 8 oxygen atoms
What is haemoglobins function
Binding oxygen in lungs and transporting the oxygen to the tissue to be used in aerobic metabolic pathways
Why can oxygen be carried efficiently
Oxygen isn’t very soluble in water and haemoglobin is
What does the Fe2+ allow when transporting haemoglobin
Allows O2 to be reversibly bind
No amino acids that make up the polypeptide chains in haemoglobin are well suited to binding with oxygen
What does the oxygen bind to
The haem groups
Whats another word for red blood cells
Erythrocytes
Equation for haemoglobins binding to oxygen
Oxygen + Haemoglobin <-> Oxyhaemoglobin
4O2 + Hb <-> Hb4O2
Process name of O2 binding
Cooperative bindig
Describe cooperative binding
Binding of first O2 molecule results in conformational change in the structure of the haemoglobin molecule
so its easier for each successive O2 to bind
How are red blood cells adapted for O2 transport
Red blood cells lack nuclei = more space for haemoglobin
Biconcave shape = high SA:V, so there is a short diffusion distance for O2