CONFORMATIONAL CHANGES IN HEME PROTEINS AND MODEL COMPOUNDS
Open Access
- 1 December 1976
- journal article
- Published by EDP Sciences in Le Journal de Physique Colloques
- Vol. 37 (C6) , C6-195
- https://doi.org/10.1051/jphyscol:1976641
Abstract
Zero-field Mössbauer spectra of oxygenated hemoglobin, myoglobin and some of their model compounds were recorded at various températures. Each sample gave rise to quadrupole doublet with temperature-dependent linewidth and quadrupole splitting. We have compared the native protein spectra with the spectra from one of the model compounds extensively studied by Mössbauer spectroscopy, and we conclude that oxygen relaxation between conformational states is responsible for the temperature dependence in both casesKeywords
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