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Can a two-state MWC allosteric model explain hemoglobin kinetics?

E R Henry1, C M Jones, J Hofrichter

  • 1Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland 20892-0520, USA.

Biochemistry
|May 27, 1997
PubMed
Summary
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This study refines the Monod-Wyman-Changeux (MWC) allosteric model for hemoglobin, incorporating ligand rebinding and tertiary relaxation. The enhanced model accurately explains complex kinetic and equilibrium data, validating its critical tests.

Area of Science:

  • Biophysics
  • Biochemistry
  • Physical Chemistry

Background:

  • Hemoglobin's ligand binding kinetics and conformational changes are crucial for oxygen transport.
  • Existing allosteric models require refinement to capture complex molecular dynamics.

Purpose of the Study:

  • To analyze nanosecond-millisecond kinetics of ligand binding and conformational changes in hemoglobin.
  • To extend and validate the two-state allosteric model (MWC) for hemoglobin dynamics.

Main Methods:

  • Time-resolved optical spectroscopy following photodissociation of heme-carbon monoxide complex.
  • Development of an extended MWC model incorporating geminate rebinding and tertiary relaxation.
  • Utilizing linear free energy relations and concepts from myoglobin studies.

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Main Results:

  • The extended MWC model, with 85 coupled differential equations, quantitatively fits complex kinetic data.
  • The model simultaneously explains equilibrium ligand binding and ligation state distributions.
  • Model parameters successfully explain both kinetic and equilibrium experimental data.

Conclusions:

  • The refined two-state MWC allosteric model provides a comprehensive explanation for hemoglobin's kinetic and equilibrium behavior.
  • The model's success in fitting diverse datasets validates its applicability and robustness.
  • This work strengthens the MWC model's foundation in understanding allosteric regulation in proteins.