1 way in which the structure of haemoglobin is related to its function

Question

anonymous · Answer

thanks

anonymous · Answer

If you can disseminate scientific articles like this, its pretty impressive. Hemoglobin is a tetramer with 4 protein subunits (two different types) Myoglobin is an example of that has one monomer but performs similar functions Hemoglobin has a heme group (Iron) that is needed for the active site where EITHER molecular oxygen or carbon dioxide bind to. Here is an example of how the heme group looks like: http://upload.wikimedia.org/wikipedia/commons/b/be/Heme_b.svg Well those are some relevant information, if you can piece them together you will have a good answer!

aaronq · Answer

The subunits also exhibit cooperative binding, i.e. when one heme group binds dioxygen it changes conformation such that the affinity for dioxygen of another subunit increases. At high $P_{O_2}$ in blood (i.e. lungs) all heme's are bound to dioxygen, and as $P_{O_2}$ decreases (as it travels down your blood stream) the affinity decreases, so all oxygen is unloaded at $O_2$ deficient tissues.

abb0t · Answer

I remember that graph from Structural Biochem. Lol

anonymous · Answer

thanks for the help guys

anonymous · Answer

The shape allows it to bind to oxygen molecules better.