Multiplicity of interactions between dromedary hemoglobin and solvent components

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Abstract
The interaction of dromedary hemoglobin with various solvent components [2‐(p‐chlorophenoxy)‐2‐methylpropionic acid (CFA), 2,3‐bisphospho‐D‐glycerate (glycerate‐2,3‐P2) and chloride] has been studied. 1 CFA greatly lowers the oxygen affinity of dromedary hemoglobin. 2 The oxygen‐linked CFA binding sites are probably located in the deoxy derivative at the α cleft, while in the oxy form and in the presence of two other effectors (glycerate‐2,3‐P2 and chloride) additional, structurally and possibly functionally relevant binding site(s) should be considered. 3 Both CFA and glycerate‐2,3‐P2 stabilize the deoxy‐like tertiary structure in the oxy derivative. 4 Chloride appears to be fundamental to obtain quaternary structural changes. 5 Interaction energy, retained in the protein when the three ligands (CFA, glycerate‐2,3‐P2 and chloride) are bound to the oxy form, favours intermediates not stable if only one or two allosteric effector(s) is (are) present on the protein. 6 The oxygen affinity appears to be related to both tertiary and quaternary structural changes, while cooperativity is largely invariant with solvent conditions. In conclusion, the functional properties of dromedary hemoglobin do not depend in any simple way on the variety of stabilized conformations.

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