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Related Concept Videos

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Oxidative Cleavage of Alkenes: Ozonolysis

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Oxygenic Photosynthesis01:26

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IR and UV–Vis Spectroscopy of Aldehydes and Ketones01:29

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Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
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Oxidative interaction between OxyHb and ATP: a spectroscopic study.

Mousumi Banerjee1, Abhijit Chakrabarti, Samita Basu

  • 1Chemical Sciences Division, Saha Institute of Nuclear Physics, Kolkata, India.

The Journal of Physical Chemistry. B
|May 10, 2012
PubMed
Summary

Adenosine triphosphate (ATP) binds to oxyhemoglobin (oxyHb), decreasing oxygen affinity and forming methemoglobin (metHb). This interaction is enthalpy-driven, involving hydrogen bonds and van der Waals forces.

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Area of Science:

  • Biochemistry
  • Biophysics
  • Spectroscopy

Background:

  • Oxyhemoglobin (oxyHb) is the oxygenated form of hemoglobin, crucial for oxygen transport.
  • Adenosine triphosphate (ATP) is the primary energy currency of cells.
  • Understanding molecular interactions is key to physiological processes.

Purpose of the Study:

  • To elucidate the binding mode between oxyhemoglobin and adenosine triphosphate.
  • To investigate the impact of ATP binding on oxyhemoglobin's structure and function.
  • To determine the thermodynamic and kinetic parameters of the oxyHb-ATP interaction.

Main Methods:

  • Absorption and fluorescence spectroscopy were employed to study the binding.
  • Circular dichroism and synchronous fluorescence spectroscopy assessed structural changes.
  • Theoretical molecular docking provided insights into the binding site.

Main Results:

  • A ground state complex formation between oxyHb and ATP was observed, evidenced by isosbestic points.
  • The binding constant was determined to be 3.8 × 10(3) M(-1) at 25 °C.
  • ATP binding led to decreased oxygen affinity and induced methemoglobin formation, indicating an oxidative interaction.

Conclusions:

  • The oxyHb-ATP interaction is enthalpy-driven, primarily mediated by hydrogen bonds and van der Waals forces.
  • ATP binding induces conformational changes in oxyHb, affecting its oxygen-carrying capacity.
  • This study provides molecular-level understanding of ATP's influence on hemoglobin function.