High-field (94-GHz) EPR spectroscopy on the S(2) multiline signal of Photosystem II

FEBS Lett. 2006 Jun 26;580(15):3605-9. doi: 10.1016/j.febslet.2006.05.039. Epub 2006 May 24.

Abstract

The multiline signal of the S(2) state in Photosystem II was measured both in frozen-solution and single-crystal preparations from the cyanobacterium Thermosynechococcus elongatus. The frozen-solution EPR spectrum shows a gaussian-like line shape without any resolution of Mn hyperfine couplings. This line shape can be understood on the basis of the single-crystal spectra, where a strong orientation dependence of partially resolved hyperfine structures appears. Simulation of the frozen-solution spectrum on the basis of Mn hyperfine couplings taken from published pulse-ENDOR data yields a fully rhombic g-matrix for the multiline signal with principal components 1.997, 1.970, and 1.965. The resulting isotropic g-value g(iso)=1.977 is surprisingly small compared to other manganese complexes containing manganese ions in the formal oxidation states three and four.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Cyanobacteria / chemistry
  • Electron Spin Resonance Spectroscopy
  • Photosystem II Protein Complex / chemistry*
  • Solutions

Substances

  • Photosystem II Protein Complex
  • Solutions