6. Bird hemoglobin are tetrameric and very similar in structure and function to

Question

6. Bird hemoglobin are tetrameric and very similar in structure and function to mammalian hemoglobins. However, in some bird species, O, binding affinity to hemoglobin is not regulated by 2,3-BPG, but rather by a different compound that functions as a 2,3-BPG analog a) Considering the chemical and physical properties of the following compounds, which is the most likely candidate for the 2,3-BPG analog in bird red blood cells? OPO CH OH OPC, ?? 0 NH ?? OPO OH OP03 b) The bird 2,3-BPG analog binds to hemoglobin in the same way 2,3-BPG binds to mammalian hemoglobin. Briefly describe where in the structure of the tetrameric bird hemoglobin you would expect the compound to bind and by what type of bonds and/or interactions. c) Would you expect the compound to increase or decrease the O, binding affinity of bird hemoglobin?

Explanation / Answer

1. The second compound that is inositol hexaphosphate will act as a functional analog for the 2, 3-BPG because it can have a negative charge and can function like to 2, 3-BPG.

2. The compound binds similar to 2, 3- BPG, that means inside the central cavity of the haemoglobin interacting with histidine, lysine and the N-terminus of the haemoglobin molecule. The compound would bind to the tetramer with ionic interactions similar to 2, 3-BPG.

3. The inositol hexaphosphate will increase the oxygen binding affinity and will decrease the dissociation of oxygen due to the presence of the phosphate-rich environment.

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