Carbon Monoxide Binding in a Model of Hemoglobin Differs Between the T and the R Conformation

  • Jacob P. Zock
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 277)


Carbon monoxide impedes the transport of oxygen in blood by competitive binding to the oxygen binding sites on hemoglobin. The affinity of these sites for carbon monoxide is much greater than that for oxygen. The ratio between carbon monoxide affinity and oxygen affinity (M) is usually assumed to have a fixed value (Haldane’s law), which is about 200. Reported values differ between authors (Douglas et al., 1912, Killick, 1936, Sendroy et al., 1929). However, this ratio is not a constant but depends on the level of saturation (Roughton, 1970) as well as on pH (Joels and Pugh, 1958). This means that simple procedures cannot be used to calculate the combined effects of simultaneous oxygen and carbon monoxide binding. Application of our mathematical model of hemoglobin (Zock, 1987) shows that this model can account for the above-mentioned phenomena in a straightforward way.


Carbon Monoxide Competitive Binding Equilibrium Curve Oxygen Affinity Human Hemoglobin 
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Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Jacob P. Zock
    • 1
  1. 1.Dept. of Physiology, School of MedicineUniversity of GroningenGroningenThe Netherlands

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