0000000000291943
AUTHOR
Beate Meier
The active center of superoxide dismutase from Propionibacterium shermanii
A self-consistent description of the EPR spectra and of the Mossbauer spectra of the natural superoxide dismutase from Propionibacterium shermanii with ferric iron as an active centre is presented. The spectra were measured at pH 6.5, 7.8 and 9.4. The theoretical approach is based on the use of the complete crystal field Hamiltonian for the high-spin ferric complexes with due regard for the terms of the fourth power of the electronic spin. It is shown that a SOD molecule can exist in two conformations. The low-pH conformation has predominantly trigonal symmetry, while the high-pH conformation has the symmetry close to the «extreme rhombic». This interpretation is in full agreement with EXAF…
An interpretation of EPR spectra of azide ligated superoxide dismutase from Propionibacterium shermanii
A self-consistent description of the EPR spectra of the azide ligated SOD is obtained by taking into account the general configuration of the crystal field splitting in the crystal field Hamiltonian. The spread in the rhombicity parameter due to the presence of different conformational substates is introduced.