Redox potentials of normal and SH(beta 93)-modified human hemoglobin. Effect of pH and D-glycerate 2,3-bisphosphate.

The effect of pH and D-glycerate 2,3-bisphosphate on the oxidation-reduction equilibria of human hemoglobin, normal and modified at the SH(beta 93) groups by reaction with cystine dimethylester has been studied with the aim of comparing the redox equilibria with the oxygen equilibria previously studied under the same experimental conditions. Analysis of data has shown that: (i) the same groups are involved in the oxygenation and oxidation alkaline Bohr effect; (ii) the pK values of these groups are lower in met-hemoglobin than in oxyhemoglobin; (iii) the difference in the affinity for D-glycerate 2,3-bisphosphate of ferric and deoxyhemoglobin is pH-independent in the normal protein, while significantly decreasing with a decrease in pH in the modified protein; (iv) the high cooperativity of the redox process (also occurring at acid pH) and the reduced oxidation Bohr effect observed in the modified protein are consistent with the destabilization of the T structure induced by the bulky reagent bound to the SH(beta 93) groups of the protein.