Co-binding studies on Hb M Iwate. Allostery of a T state haemoglobin.
The mutant haemoglobin Hb M Iwate alpha 2Mmet87His leads to Tyr beta 2, is characterized by a stable T structure and a low ligand affinity. Sigmoidal CO-binding isotherms of symmetrical shape with Hill coefficients of n = 1.4 at pH 6 to n = 1.9 at pH 10 and the differences in the mean affinity (PCO(1/2)) and the affinity of the first ligand-binding beta subunit (1/L1 greater than Pco(1/2)) are the evidence for the cooperativity. The comparison of the Bohr effects of the two valency hybrid states (alpha 2Mmet beta met beta deoxy alpha 2Mmet beta 2deoxy) in the absence of and in the presence of polyphosphates leads to an indirect proof of pH-dependent subunit-subunit interaction. Inositol hexaphosphate-binding suppresses cooperativity in the pH range 5.5-8 (n = 1). Above pH 8 hte cooperativity increases to a final value of n = 1.9 at pH greater than 10, which is identical to that of stripped Hb M Iwate. The CO binding to the first binding site exhibits a Bohr effect. Polyphosphate anions have no influence on the CO binding of the first binding site. The heterotropic effects are discussed as intrachain effects (Bohr effect of the first binding site) and interchain effects (Bohr effect of Pco(1/2); influence of polyphosphates).
D000494:Allosteric Regulation; D000495:Allosteric Site; D002248:Carbon Monoxide; D002263:Carboxyhemoglobin; D006449:Hemoglobin M; D006455:Hemoglobins, Abnormal; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008024:Ligands; D008433:Mathematics; D010108:Oxyhemoglobins; D010833:Phytic Acid; D011485:Protein Binding; D011487:Protein Conformation
D006455:Hemoglobins, Abnormal; D008024:Ligands; D010108:Oxyhemoglobins; D010833:Phytic Acid; D002248:Carbon Monoxide; D002263:Carboxyhemoglobin; D006449:Hemoglobin M