Coupling of the oxygen-linked interaction energy for inositol hexakisphosphate and bezafibrate binding to human HbA0.

@article{Coletta1999CouplingOT,
  title={Coupling of the oxygen-linked interaction energy for inositol hexakisphosphate and bezafibrate binding to human HbA0.},
  author={Massimo Coletta and Mauro Angeletti and Paolo Ascenzi and Alberto Bertollini and S. Della Longa and Giampiero de Sanctis and Anna Maria Priori and R N Tibetha Santucci and Gino Amiconi},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 11},
  pages={
          6865-74
        }
}
The energetics of signal propagation between different functional domains (i.e. the binding sites for O2, inositol hexakisphospate (IHP), and bezafibrate (BZF)) of human HbA0 was analyzed at different heme ligation states and through the use of a stable, partially heme ligated intermediate. Present data allow three main conclusions to be drawn, and namely: (i) IHP and BZF enhance each others binding as the oxygenation proceeds, the coupling free energy going from close to zero in the deoxy… CONTINUE READING

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