Hæmoglobin and Myoglobin: Cooperativity

  • Engelbert Buxbaum


Myoglobin is a protein with a single hæme group, which binds oxygen inside our cells and makes it available for metabolism. Oxygen binding to myoglobin is described by a hyperbola. Hæmoglobin consists of two \(\upalpha\),\(\upbeta\)-protomers, each of the four proteins contains a hæme group. Binding of oxygen to one of these hæme groups increases the affinity of the remaining sites for oxygen; this cooperation results in an S-shaped (sigmoidal) binding curve. The shape of this curve is influenced by pH and the presence of 2,3-Bisphosphoglycerate (2,3-BPG). Mutations in the genes for either the \(\upalpha\)- or the \(\upbeta\)-subunits of hæmoglobin can cause serious disease.


Oxygen Partial Pressure Sickle Cell Oxygen Affinity Oxygen Binding Binding Curve 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


  1. 1.
    R. Benesch, R.E. Benesch, Intracellular organic phosphates as regulators of oxygen release by haemoglobin. Nature 221, 618–622 (1969). doi: 10.1038/221618a0 CrossRefPubMedGoogle Scholar
  2. 2.
    C. Bohr, Absorptionscoëfficiententen des Blutes und des Blutplasmas für Gase. Skand. Arch. Physiol. 17, 104 (1905). doi: 10.1111/j.1748-1716.1905.tb00547.x CrossRefGoogle Scholar
  3. 3.
    M.J. Bouva, C.L. Harteveld, P. van Delft, P.C. Giordano, Known and new delta globin gene mutations and their diagnostic significance. Haematologica 91(1), 129–132 (2006). URL
  4. 4.
    J.-P. Changeux, S. Edelstein, Conformational selection or induced fit? 50 years of debate resolved. F1000 Biol. Rep. 3(19), (2011). doi: 10.3410/B3-19
  5. 5.
    A.W. Fenton, Allostery: an illustrated definition for the ‘second secret of life’. TIBS 33(9), 420–425 (2008). doi: 10.1016/j.tibs.2008.05.009 PubMedCentralPubMedGoogle Scholar
  6. 6.
    P.R. Gardner, Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases. J. Inorg. Biochem. 99(1), 247–266 (2005). doi: 10.1016/j.jinorgbio.2004.10.003 CrossRefPubMedGoogle Scholar
  7. 7.
    P.R. Gardner, A.M. Gardner, L.A. Martin, A.L. Salzman, Nitric oxide dioxygenase: An enzymic function for flavohemoglobin. Proc. Natl. Acad. Sci. USA 95(18), 10378–10383 (1998). URL
  8. 8.
    M.T. Gladwin, J.H. Crawford, R.P. Patel, The biochemistry of nitric oxide, nitrite, and hemoglobin: role in blood flow regulation. Free Radical Biol. Med. 36(6), 707–717 (2004).  10.1016/j.freeradbiomed.2003.11.032 CrossRefGoogle Scholar
  9. 9.
    A.V. Hill, The possible effects of the aggregation of the molecules of hæmoglobin on its dissociation curves. J. Physiol. 40, 190 (1910)PubMedCentralCrossRefPubMedGoogle Scholar
  10. 10.
    O. Hofmann, R. Mould, T. Brittain, Allosteric modulation of oxygen binding to the three human embryonic hæmoglobins. Biochem. J. 306, 367–370 (1995). URL
  11. 11.
    D.E. Koshland, G. Nemethy, D. Filmer, Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 4, 365–385 (1966). doi: 10.1021/bi00865a047. URL
  12. 12.
    J. Monod, J. Wyman, J.P. Changeux, On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12, 88–118 (1965). doi: 10.1016/S0022-2836(65)80285-6 CrossRefPubMedGoogle Scholar
  13. 13.
    G.R. Serjeant, B.E. Serjeant, Sickle Cell Disease, 3rd edn. (Oxford University Press, Oxford, 2001). ISBN 978-0-1926-3036-0Google Scholar

Copyright information

© Springer International Publishing Switzerland 2015

Authors and Affiliations

  • Engelbert Buxbaum
    • 1
  1. 1.KevelaerGermany

Personalised recommendations