Allosteric effect of o-iodobenzoate on hemoglobin.
O-Iodobenzoate interacts non-covalently with hemoglobin and lowers the oxygen affinity of the protein. In contrast to 2,3-diphosphoglycerate or inositol hexaphosphate, its interaction does not depend upon the presence of free amino groups at the beta-chain amino terminals. Lysine beta82 is one of its oxygenation linked binding sites. As with the organic phosphates, the halogenated benzoate reacts preferentially with deoxy-hemoglobin to shift the allosteric equilibrium from R to T.
D000494:Allosteric Regulation; D006454:Hemoglobins; D007463:Iodobenzoates / Q000494:pharmacology*; D010100:Oxygen; D010108:Oxyhemoglobins
D006454:Hemoglobins; D007463:Iodobenzoates; D010108:Oxyhemoglobins; D010100:Oxygen