Assembly and disassembly of the photosystem II manganese cluster reversibly alters the coupling of the reaction center with the light-harvesting phycobilisome

Biochemistry. 2008 Sep 16;47(37):9747-55. doi: 10.1021/bi800568p. Epub 2008 Aug 22.

Abstract

The light-driven oxidative assembly of Mn (2+) ions into the H 2O oxidation complex (WOC) of the photosystem II (PSII) reaction center is termed photoactivation. The fluorescence yield characteristics of Synechocystis sp. PCC6803 cells undergoing photoactivation showed that basal fluorescence, F 0, exhibited a characteristic decline when red, but not blue, measuring light was employed. This result was traced to a progressive increase in the coupling of the phycobilisome (PBS) to the PSII reaction center as determined by observing the changes in room temperature and 77 K fluorescence emission spectra that accompany photoactivation. The results support the hypothesis that strong energetic coupling of the PBS to the PSII reaction center depends upon the formation of an active WOC, which presumably diminishes the likelihood of photodamage to reaction centers that have either lost an intact Mn cluster or are in the process of assembling an active WOC.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Kinetics
  • Light
  • Light-Harvesting Protein Complexes / chemistry
  • Light-Harvesting Protein Complexes / metabolism
  • Manganese / chemistry*
  • Manganese / metabolism*
  • Oxidation-Reduction
  • Photolysis
  • Photosystem II Protein Complex / chemistry*
  • Photosystem II Protein Complex / metabolism*
  • Phycobilisomes / metabolism*
  • Spectrometry, Fluorescence
  • Synechocystis / metabolism
  • Water / chemistry

Substances

  • Light-Harvesting Protein Complexes
  • Photosystem II Protein Complex
  • Phycobilisomes
  • Water
  • Manganese