Oxygen equilibrium curves of the dimeric and tetrameric hemoglobin components of Scapharca inaequivalvis were determined at several temperatures. The oxygen equilibrium curves were analyzed by the two-step and four-step oxygen equilibrium schemes of Adair for the dimeric and tetrameric hemoglobins, respectively. The enthalpy and entropy changes for each oxygenation step were determined by the temperature dependences of the Adair constants using van't Hoff equations. Neither dimeric nor tetrameric hemoglobins release protons or anions upon oxygenation under the experimental conditions of the present study. The enthalpy and entropy changes are non-uniform with respect to the oxygenation step and do not need to be corrected for the oxygenation-linked release of protons and anions. For the tetrameric hemoglobin, enthalpy-entropy compensation was observed between the first, second and third steps of oxygenation. The present results suggest that the origin of the co-operative oxygenation is primarily entropic for both hemoglobin components of S. inaequivalvis. Comparison of these data with those obtained on other hemoglobins shows that no simple generalization can be made as to the thermodynamic nature of co-operativity in oxygen binding.
ASJC Scopus subject areas