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Haem-apoprotein interactions detected by resonance Raman scattering in Mb- and Hb-derivates lacking the saltbridge His146 beta-Asp94 beta
Journal article   Peer reviewed

Haem-apoprotein interactions detected by resonance Raman scattering in Mb- and Hb-derivates lacking the saltbridge His146 beta-Asp94 beta

S el Naggar, W Dreybrodt and R Schweitzer-Stenner
European biophysics journal, v 12(1)
1985
PMID: 4006878

Abstract

Animals Apoproteins - metabolism Aspartic Acid Heme - metabolism Hemoglobins - metabolism Histidine Hydrogen-Ion Concentration Myoglobin - metabolism Spectrum Analysis, Raman Structure-Activity Relationship Whales
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) beta and Asp(FG5) beta, which is essential for the cooperativity in the haemoglobin system.

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Biophysics
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