Abstract
The dispersion of the depolarization ratio of oxidation- and spin-marker lines of sperm whale myoglobin derivatives (oxyMb, deoxyMb, ferric Mb-CN) and of ferric Hb-CN have been measured for different pH-values in the acid and alkaline region. No pH-dependence in the region above pH=6.5 has been found. Below pH=6.5, however, a significant pH-dependence of the oxyMb-oxidation marker line at 1,375 cm-1 exists. Additionally, a weak pH-dependence of the corresponding 1,355 cm-1 line of the deoxymyoglobin spectrum is observed. This effect can be explained assuming a titration of distal histidine, inducing a rupture of the ligand-imidazole H-bond in the case of oxymyoglobin. The pH-independent depolarization ratio disperson above pH=6.5 in all systems investigated is explained by the lack of the haemoglobin saltbridge between His(HC3)β and Asp(FG5)β, which is essential for the cooperativity in the haemoglobin system.
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Abbreviations
- DPR:
-
depolarization ratio
- EP:
-
excitation profile
- oxyMb:
-
oxymyoglobin
- deoxyMb:
-
deoxymyoglobin
- metMb-CN:
-
ferric myoglobincyanide
- metHb-CN:
-
ferric haemoglobincyanide
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el Naggar, S., Dreybrodt, W. & Schweitzer-Stenner, R. Haem-apoprotein interactions detected by resonance Raman scattering in Mb- and Hb-derivates lacking the saltbridge His146β-Asp94β. Eur Biophys J 12, 43–49 (1985). https://doi.org/10.1007/BF00254094
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DOI: https://doi.org/10.1007/BF00254094