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Anionic binding site and 2,3-DPG effect in bovine hemoglobin

M Marta1, M Patamia, A Colella

  • 1Istituto di Chimica e Chimica Clinica, Centro CNR per la Chimica dei Recettori, UCSC, Facoltà di Medicina, Roma, Italy.

Biochemistry
|October 7, 1998
PubMed
Summary
This summary is machine-generated.

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Bovine hemoglobin (BvHb) interacts with 2,3-diphosphoglycerate (2,3-DPG) even with chloride present. This interaction, confirmed by NMR and oxygen binding, challenges previous beliefs and suggests synergistic effects influencing BvHb

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Physiology

Background:

  • Bovine hemoglobin (BvHb) was previously thought to interact weakly with 2,3-diphosphoglycerate (2,3-DPG) in chloride-free media and not at all in the presence of physiological chloride concentrations.
  • This perceived lack of interaction raised questions regarding structural and evolutionary aspects of BvHb-2,3-DPG binding.

Purpose of the Study:

  • To investigate the interaction between bovine hemoglobin and 2,3-diphosphoglycerate in the presence of physiological chloride concentrations.
  • To elucidate the functional consequences of this interaction on oxygen binding affinity.

Main Methods:

  • 31P nuclear magnetic resonance (NMR) spectroscopy to detect 2,3-DPG binding to BvHb.
  • Oxygen binding experiments to assess the functional impact of 2,3-DPG and chloride on BvHb oxygen affinity.

Related Experiment Videos

Main Results:

  • 31P NMR confirmed that 2,3-DPG interacts with bovine deoxy-hemoglobin even in 100 mM chloride.
  • Oxygen binding studies revealed a synergistic effect between chloride and 2,3-DPG in modulating BvHb oxygen affinity.
  • Findings suggest structural bases for this synergy, potentially involving conformational changes and an identified chloride binding site.

Conclusions:

  • Bovine hemoglobin actively reacts with 2,3-DPG and is functionally influenced by it, contrary to prior assumptions.
  • The low intraerythrocytic concentration of 2,3-DPG in adult bovines is likely an adaptive metabolic trait, not solely explained by amino acid sequence differences at the binding site.