(C) (C) (C)

Haemoproteins I: Structures and oxygenation equilibria. Haemoproteins II: Co-operative oxygen binding to haemoglobin, binding of CO2 and H+. Allosteric effects. Binding of CO. Haemoproteins III: Molecular diseases and mutant haemoglobins.

SAQs: 1. Haemoglobin is the oxygen transport protein in the blood. (a) Draw the structure of one of the metal ions and its coordinating atoms in oxyhaemoglobin.

(b) Draw energy level diagrams for haemoglobin and oxyhaemoglobin that show the splitting energy, spin state and numbers of unpaired electrons on the metal ion?

(c) What is an allosteric protein?

(d) Give examples of allosteric effects in Haemoglobin.

2.

The distal histidine in haemoglobin plays a life-saving role in discriminating between CO and O2 binding.

(i) Using representations of the structures of the CO and O2 complexes with a haemoglobin subunit explain what this role is.

(ii) Why is the decrease in relative affinities life-saving?

MCQs: 1. In which of the following haemoproteins is the metal cordinatively unsaturated? A B C D E 2. A B C D E 3. A B C D E Methaemoglobin. Metmyoglobin Myoglobin. Oxymyoglobin. Oxyhaemoglobin. In the structure of haemoglobin A salt bridge interactions occur between: all globin chains. both chains only. both chains only. each chain and a chain. each chain and both chains. Metmyoglobin is which form of myoglobin? Myoglobin which is oxidised on the porphyrin ring. The iron(III) form of myoglobin. The O2 complex of the iron(III) form of myoglobin. The same as myoglobin. The same as oxymyoglobin.