Correlation of pH-dependent resonance Raman and optical absorption data reflecting haem-apopprotein interaction in oxy haemoglobin
Author:
Publisher
Elsevier BV
Subject
Inorganic Chemistry,Organic Chemistry,Spectroscopy,Analytical Chemistry
Reference5 articles.
1. R. Schweitzer-Stenner, W. Dreybrodt, D. Wedekind, and U. Kubitscheck, J. Mol. Struct., this issue
2. Excitation profiles and depolarization ratios of some prominent Raman lines in oxyhaemoglobin and ferrocytochrome c in the pre-resonant and resonant region of the Q-band
3. Investigation of pH-induced symmetry distortions of the prosthetic group in oxyhaemoglobin by resonance Raman scattering
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1. Near-Infrared Spectrometric Determination of Blood pH;Journal of Surgical Research;2002-08
2. Characterization of pH Variation in Lysed Blood by Near-Infrared Spectroscopy;Applied Spectroscopy;1998-03
3. Raman dispersion spectroscopy probes heme distortions in deoxyHb-trout IV involved in its T-state Bohr effect;Biophysical Journal;1993-04
4. Allosteric linkage-induced distortions of the prosthetic group in haem proteins as derived by the theoretical interpretation of the depolarization ratio in resonance Raman scattering;Quarterly Reviews of Biophysics;1989-11
5. The influence of structural variations in the F- and FG-helix of the β-subunit modified oxyHb-NES on the heme structure detected by resonance Raman spectroscopy;European Biophysics Journal;1989-06
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