A New Model of Hemoglobin Oxygenation.

Entropy (Basel)

Laboratory of DNA-Protein Interactions, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilova Str. 32, 119991 Moscow, Russia.

Published: August 2022

AI Article Synopsis

  • The study explores how hemoglobin binds to oxygen, highlighting the cooperative nature of this process based on earlier works by Hill.
  • The Adair model is noted for better fitting experimental data, though its parameter meanings are still not fully understood.
  • The researchers improved upon Hill's approach by using a Lorentz distribution for oxygen partial pressure, resulting in a model that more accurately describes the experimental data than both the Hill and Adair equations.

Article Abstract

The study of hemoglobin oxygenation, starting from the classical works of Hill, has laid the foundation for molecular biophysics. The cooperative nature of oxygen binding to hemoglobin has been variously described in different models. In the Adair model, which better fits the experimental data, the constants of oxygen binding at various stages differ. However, the physical meaning of the parameters in this model remains unclear. In this work, we applied Hill's approach, extending its interpretation; we obtained a good agreement between the theory and the experiment. The equation in which the Hill coefficient is modulated by the Lorentz distribution for oxygen partial pressure approximates the experimental data better than not only the classical Hill equation, but also the Adair equation.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9498255PMC
http://dx.doi.org/10.3390/e24091214DOI Listing

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