Dynamics of Structural Changes in Hemoglobin

  • Eric R. Henry
  • James Hofrichter
  • William A. Eaton
Conference paper
Part of the Springer Series in Biophysics book series (BIOPHYSICS, volume 1)


Upon dissociation of oxygen or carbon monoxide hemoglobin undergoes a series of conformational changes that are responsible for its cooperative behavior. X-ray structural studies show that these changes include a displacement of the iron from the heme plane and a tilt of the proximal histidine associated with a shift in the F helix (1–3). This shift destabilizes the intersubunit bonding between α β dimers, and after dissociation of one or two ligands the strain at the interface is sufficient to cause a transition from the R quaternary structure to the T quaternary structure.


Quaternary Structure Resonance Raman Spectrum Geminate Recombination Ligand Dissociation Cobalt Porphyrin 
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Copyright information

© Springer-Verlag Berlin Heidelberg 1987

Authors and Affiliations

  • Eric R. Henry
    • 1
  • James Hofrichter
    • 1
  • William A. Eaton
    • 1
  1. 1.Laboratory of Chemical PhysicsNIDDK, National Institutes of HealthBethesdaUSA

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