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Oxygen transport

Haemoglobin, Myoglobin, Buffering systems

QuestionAnswer
State the Henderson Hasselbalch equation pH = pKa + (log[A-]/[HA])
Describe the haem molecule Porphyrin molecule to which an iron atom (Fe2+) is coordinated; the porphyrin ring is a complex C-N structure
How is haem attached to globin and what does this do? Attached to the globin chain through proximal histidine residue prevents oxidation of iron to higher oxidation states
Why is haem protected by the globin polypeptide? Minimises spontaneous oxidation of Fe2+ to Fe 3+
How does O2 binding change the shape of haemoglobin? Heme assumes a planar configuration and the central iron atom occupies a space in the plane o the heme group
Describe the shape of deoxygenated heme Heme is domed: iron atom in the center is drawn out of the plane
How does the O2 binding change the shape of deoxyhaemoglobin? Binding of O2 causes conformational changes which lead to breakage of some of the non-covalent interactions between subunits
Describe the co-operative binding of O2 to Hb Each subunit of Hb binds O2 independently, the binding of O2 at one subunit influences the binding of O2 at other subunits
How does 2,3 BPG stabilise the tense state of haemoglobin? Binds in the cleft between subunits only present in the T-state
Describe the oxygen binding characteristics of myoglobin Myoglobin consists of alpha helices containing haem bound to two histidine residues which are involved in oxygen binding
Describe the oxygen binding characteristics of haemoglobin Haemoglobin is a tetramer with only one histidine residue involved when oxygen binds to haem. There are four haemoglobin molecules
Created by: Yanna Lai Yanna Lai on 2009-08-01



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