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2,3-DPG-Hb complex: a hypothesis for an asymmetric binding.

M Pomponi1, C Bertonati, E Fuglei

  • 1Istituto di Chimica e Chimica Clinica, UCSC, Facoltà di Medicina, Roma, Italy. m.pomponi@uniserv.ccr.rm.cnr.it

Biophysical Chemistry
|June 14, 2000
PubMed
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This study investigated the 2,3-diphosphoglycerate (2,3-DPG) binding site symmetry in hemoglobin (Hb) using 31P NMR. Results suggest an asymmetric binding site in solution, potentially explaining hemoglobin

Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • The binding site of 2,3-diphosphoglycerate (2,3-DPG) in hemoglobin (Hb) has been proposed to be symmetrical.
  • Previous crystallographic studies suggested a symmetrical 2,3-DPG binding site in deoxy-Hb crystals.

Purpose of the Study:

  • To investigate the symmetry of the 2,3-DPG binding site in hemoglobin (Hb) in solution.
  • To explore the impact of pH and Hb type on 2,3-DPG binding.

Main Methods:

  • 31P nuclear magnetic resonance (NMR) spectroscopy was used to study the interaction of 2,3-DPG with Hb.
  • Experiments were conducted using Hb from various species, including humans, polar bears, Arctic foxes, and bovines.

Main Results:

Related Experiment Videos

  • The chemical shifts of 2,3-DPG's P2 and P3 resonances were dependent on both pH and Hb type.
  • 2,3-DPG binds tightly to deoxyhemoglobin and weakly but significantly to oxyhemoglobin.
  • Results indicate a loss of symmetry in the 2,3-DPG binding site in solution, suggesting differences in quaternary structure among deoxy-Hb forms.

    • Conclusions:

    • The binding of 2,3-DPG to Hb in solution appears to be asymmetric.
    • This asymmetry may correlate with Hb's functional behavior and explain physiological differences.
    • Solution studies are crucial for understanding the functional effects of 2,3-DPG on Hb.