Correspondence of the pK values of oxyHb-titration states detected by resonance Raman scattering to kinetic data of ligand dissociation and association.
The dispersion of the depolarization ratio of oxidation and spinmarker lines of oxyhemoglobin at low C1- concentration (less than 0.08 M) have been examined for different pH values in the acid and alkaline region. Interpreting the depolarization ratio dispersion curves by fifth order Loudon theory of the polarizibility tensor, we obtain tensor parameters depending linearly on symmetry classified distortions of the functional hemegroup. The pH dependence of these parameters are explained by assuming the influence of three titrable groups with pK = 7.8, 6.6, and 5.8 on the heme. Using these pK values, we are able to interpret the pH dependence of CO(O2)-dissociation and CO-association of the fourth hemoglobin subunit. We conclude from our measurements that the change of the Tyr HC2 beta-configuration induces heme-apoprotein interaction via the Tyr HC2 beta-Val FG5 beta H-bond, which are transduced to the heme via central and peripheral coupling.
Schweitzer-Stenner
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R
Wedekind
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Dreybrodt
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D002712:Chlorides / Q000494:pharmacology; D006441:Hemoglobin A / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008433:Mathematics; D008954:Models, Biological; D010108:Oxyhemoglobins / Q000378:metabolism*; D013059:Spectrum Analysis, Raman / Q000379:methods; D013816:Thermodynamics
D002712:Chlorides; D010108:Oxyhemoglobins; D006441:Hemoglobin A; C029774:oxyhemoglobin A