An electrochemical investigation of effect of ATP on hemoglobin Original Research Article

The titratable potentiometric response of hemoglobin (Hb) induced by adenosine-5′-triphosphate (ATP) is observed. The concentration-dependent effect of ATP on the anaerobic redox reaction of the protein at pH 7.0 reflects that ATP will induce stabilization of the reduced state and destabilization of the R-like (met Fe(III)) state of the metHb, when ATP concentration is lower than 3.0 mM. But when ATP concentration is between 4 and 7 mM, shift of the oxidation potential may also be observed. With reference to the study of adenosine, adenosine-5′-monophosphate, adenosine-5′-diphosphate and 2,3-diphosphoglycerate, the allosteric effect of ATP on Hb is discussed extensively. This study has given an electrochemical approach to the investigation of effect of ATP, an in vivo allosteric effector, on Hb in the physiological concentration range.