Journal article
Correspondence of the pH values of OXYHB-titration states detected by resonance raman scattering to kinetic data of ligand dissociation and association
Biophysical journal, Vol.49(5), pp.1077-1088
01 Jan 1986
Abstract
The dispersion of the depolarization ratio of oxidation and spinmarker lines of oxyhemoglobin at low Cl super(-) concentration (< 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 London theory of the polarizibility tensor, the authors 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, the authors are able to interpret the pH dependence of CO(O sub(2))-dissociation and CO-association of the fourth hemoglobin subunit. The authors conclude from their 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.
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Details
- Title
- Correspondence of the pH values of OXYHB-titration states detected by resonance raman scattering to kinetic data of ligand dissociation and association
- Creators
- R Schweitzer-StennerD WedekindW Dreybrodt
- Publication Details
- Biophysical journal, Vol.49(5), pp.1077-1088
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- [Retired Faculty]
- Identifiers
- 991019196707804721