ELECTRONIC STRUCTURE OF THE IRON IN DEOXIGENATED MYOGLOBIN FROM MÖSSBAUER SPECTROSCOPY

New measurements of the temperature dependence of the quadrupole splitting of iron in deoxigenated sperm whale myoglobin are reported. The energy separation of the low lying electronic terms of the iron is obtained by a direct least squares fit to the temperature variation of the electric field grad...

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Bibliographic Details
Main Authors: Eicher, H., Parak, F., Bade, D., Tejada, J.
Format: Article in Journal/Newspaper
Language:English
Published: HAL CCSD 1974
Subjects:
Online Access:https://hal.science/jpa-00215822
https://hal.science/jpa-00215822/document
https://hal.science/jpa-00215822/file/ajp-jphyscol197435C665.pdf
https://doi.org/10.1051/jphyscol:1974665
Description
Summary:New measurements of the temperature dependence of the quadrupole splitting of iron in deoxigenated sperm whale myoglobin are reported. The energy separation of the low lying electronic terms of the iron is obtained by a direct least squares fit to the temperature variation of the electric field gradient. Taking the 5B2 term as the reference level (E = 0) the following energy scheme was deduced : lAl(60 cm-1) 5E(106 cm-1) 3E(809 cm-1) D(- 298 cm-1) yielding η(77 K) = - 13.3. These results are consistent with Mössbauer spectra of the iron in single crystals of deoxigenated myoglobin recently reported by Gonser et al.