Bird hemoglobin are tetrameric and very similar in structure and function to mam
ID: 171666 • Letter: B
Question
Bird hemoglobin are tetrameric and very similar in structure and function to mammalian hemoglobins. However, in some bird species. O_2 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? 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 binding affinity of bird hemoglobin?Explanation / Answer
a) 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 similar to 2,3-BPG.
b) The compound binds similarly to 2,3- BPG, that means inside the central cavity of the hemoglobin interacting with lysine, histidine, and the N-terminus of the hemoglobin molecule. The compound will bind to the tetramer with ionic interactions similar to 2,3-BPG.
c) The inositol hexaphosphate would increase the oxygen binding affinity and will decrease the dissociation of oxygen due to the presence of the phosphate-rich condition.
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