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Evolution of allosteric models for hemoglobin.

William A Eaton1, Eric R Henry, James Hofrichter

  • 1Laboratory of Chemical Physics, National Institute of Diabetes, Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA. eaton@helix.nih.gov

IUBMB Life
|August 19, 2007
PubMed
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The Tertiary Two-State (TTS) model best explains hemoglobin

Area of Science:

  • Biophysics
  • Protein dynamics
  • Allosteric regulation

Background:

  • Hemoglobin's cooperative oxygen binding is explained by various allosteric models.
  • Comparing Monod, Wyman, and Changeux (MWC), Cooperon, Szabo and Karplus (SK), Lee and Karplus (SKL), and Tertiary Two-State (TTS) models.

Purpose of the Study:

  • To evaluate experimental evidence supporting different allosteric models of hemoglobin.
  • To highlight the strengths of the TTS model in explaining experimental data.

Main Methods:

  • Comparison of theoretical allosteric models.
  • Analysis of nanosecond-millisecond carbon monoxide (CO) rebinding kinetics after photodissociation.
  • Hemoglobin encapsulated in silica gels to restrict conformational changes.

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Main Results:

  • Experimental evidence predominantly favors the TTS model.
  • The TTS model explains findings inconsistent with MWC, Cooperon, SK, and SKL models.
  • CO rebinding kinetics indicate liganded T-state subunits share conformations with liganded R-state subunits.

Conclusions:

  • The TTS model, positing equilibria between high (r) and low (t) affinity states in both T and R quaternary structures, is strongly supported.
  • The TTS model offers a more comprehensive structural interpretation of hemoglobin allostery.
  • Further experiments are proposed to validate additional TTS model predictions.