Ferredoxin from Halobacterium of the Dead Sea - Mössbauer and EPR spectra and comparison with mössbauer spectrum of whole cells

M. M. Werber*, E. R. Bauminger, S. G. Cohen, S. Ofer

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

Recoil-free measurements were carried out on a 2 Fe-ferredoxin, which was isolated and purified from an extreme halophile, Halobacterium of the Dead Sea. The spectrum of this ferredoxin in the oxidized state at 82 K is a superposition of two quadrupole doublets, representing two non-equivalent Fe3+ sites of equal intensity. The spectrum of the reduced ferredoxin is consistent with the presence of two pure classes of iron atoms, ferric (lower isomer shift) and ferrous (higher isomer shift). Interpretations of the recoil-free spectra are discussed. Mössbauer measurements were also carried out on frozen whole bacterial cells and the resulting spectrum was found to be quite different from that observed in the isolated ferredoxin. Tentative conclusions are reached concerning the localization of this ferredoxin in the cytosol of the Halobacteria. The EPR spectrum of the reduced ferredoxin obtained at 24 K exhibits rhombic symmetry with the following g values: 1.894, 1.984 and 2.07. These values are similar to those obtained with 2 Fe-ferredoxins of the plant type, except that the gy and gz values are somewhat higher. Both from the EPR and Mössbauer data, it is deduced that the spin relaxation times in reduced halophilic ferredoxins are faster than in the reduced plant ferredoxins.

Original languageEnglish
Pages (from-to)169-177
Number of pages9
JournalBiophysics of Structure and Mechanism
Volume4
Issue number2
DOIs
StatePublished - Jun 1978

Keywords

  • 2 Fe-Ferredoxins
  • EPR
  • Halophilic bacteria
  • Localization of ferredoxin in the cell
  • Mössbauer spectra

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