Low-temperature spectroscopy of fully active cores. Comparison with CP43, CP47,

Research output: Contribution to journalArticle

Abstract

Comparisons of absorption spectra of photosystem II (PSII) core complexes with those of isolated CP43, CP47 and D1/D2/cyt b559 complexes show broadenings and shifts upon disassembly of the PSII core material. Spectra of PSII cores isolated from plants and cyanobacteria reveal marked changes in energies and intensities of the sharp features associated with P680. Low-temperature, illumination-induced electrochromic shifts in PSII cores allow identification of an excitation localized on pheopytin-a (pheo a) in D1. A weak interaction between an exciton component of P680 and the D1 pheo a, both located near 684 nm, is suggested. MCD spectra of 5- and 6-chlorophyll a D1/D2/cytochrome b559 preparations provide links to photoactive pigments in intact PSII cores.

Details

Authors
  • Sindra Peterson Årsköld
  • Barry J Prince
  • Elmars Krausz
  • Paul Smith
  • Ron J Pace
  • Rafael Picorel
  • Mikael Seibert
Organisations
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Biological Sciences

Keywords

  • STARK SHIFTS, RESOLUTION, REACTION CENTERS, PHOTOSYSTEM-II, CRYSTAL-STRUCTURE, PROTEIN, PIGMENTS, COMPLEXES
Original languageEnglish
Pages (from-to)97-100
JournalJournal of Luminescence
Volume108
Issue number1-4
Publication statusPublished - 2004
Publication categoryResearch
Peer-reviewedYes