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Lamprey hemoglobin forms a tetramer when deoxygenated, but when the hemoglobin becomes oxygenated, the tetramer dissociated...

Lamprey hemoglobin forms a tetramer when deoxygenated, but when the hemoglobin becomes oxygenated, the tetramer dissociated into monomers. The binding of oxygen to lamprey hemoglobin is influenced by pH, and several glutamate residues on the surface of the monomers play an important role. How might glutamate residues influence the equilibrium between the monomer and tetramer form with changes in pH?

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