European Biophysics Journal

, Volume 37, Issue 6, pp 823–827 | Cite as

An alternative theoretical formula for hemoglobin oxygenation

Original Paper

Abstract

Classical models of homotropic allostery are based on the postulate that the binding sites are equivalent in their ability to interconvert between high and low affinity states, but compelling evidence exists that the subunits of human hemoglobin are not simultaneously available for oxygen equilibration, thus reducing the number of possible intermediate microstates. The incorporation of these results into the Adair scheme reveals an alternative mechanism for hemoglobin oxygenation, not based on affinity changes.

Keywords

Hemoglobin Subunits Allostery Cooperative binding Hill plot Hierarchical equilibration mechanism 

References

  1. Adair GS (1925) The hemoglobin system VI. The oxygen dissociation curve of hemoglobin. J Biol Chem 63:529–545Google Scholar
  2. Bohr C, Hasselbach KA, Krogh A (1904) Skand Arch Physiol 16:401–412Google Scholar
  3. Bolton W, Perutz MF (1970) Three dimensional fourier synthesis of horse deoxyhaemoglobin at 2.8 Å units resolution. Nature 228:551–552CrossRefADSGoogle Scholar
  4. Brzozowski A, Derewenda Z, Dodson E, Dodson G, Grabowski M, Liddington R, Skarzyn’ski T, Vallely D (1984) Bonding of molecular oxygen to T state human haemoglobin. Nature 307:74–76CrossRefADSGoogle Scholar
  5. Fermi G, Perutz MF, Shaanan B, Fourme R (1974) The crystal structure of human deoxyhaemoglobin at 1.74 Å resolution. J Mol Biol 175:159–174CrossRefGoogle Scholar
  6. Koshland DEJ, Nemethy G, Filmer D (1966) Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 5:365–385CrossRefGoogle Scholar
  7. Lindstrom TR, Ho C (1972) Functional nonequivalence of α and β hemes in human adult hemoglobin. Proc Natl Acad Sci USA 69:1707–1710CrossRefADSGoogle Scholar
  8. Michel D (2007) Cooperative equilibrium curves generated by ordered ligand binding to multi-site molecules. Biophys Chem 129:284–288CrossRefGoogle Scholar
  9. Monod J, Wyman J, Changeux J-P (1965) On the nature of allosteric transitions: a plausible model. J Mol Biol 12:88–118CrossRefGoogle Scholar
  10. Perutz MF (1970) Stereochemistry of cooperative effects in haemoglobin. Nature 228:726–739CrossRefADSGoogle Scholar
  11. Riggs AF, Gibson QH (1973) Oxygen equilibrium and kinetics of isolated subunits from hemoglobin Kansas. Proc Natl Acad Sci USA 70:1718–1720CrossRefADSGoogle Scholar
  12. Simonneaux G, Bondon A, Brunel C, Sodano P (1988) Direct observation of intermediate ligation states of hemoglobin. J Am Chem Soc 110:7637–7640CrossRefGoogle Scholar

Copyright information

© EBSA 2008

Authors and Affiliations

  1. 1.Molecular and Cellular InteractionsUniversité de Rennes 1 Rennes CedexFrance

Personalised recommendations