Thylakoid membrane protein phosphorylation leads to a decrease in connectivity between Photosystem II reaction centers

D. J. Kyle, P. Haworth, C. J. Arntzen

Research output: Contribution to journalArticlepeer-review

78 Scopus citations

Abstract

The room-temperature fluorescence induction transients from stroma-free chloroplast membranes (in the presence of 3-(3,4-dichlorophenyl)-1,1-dimethylurea) have been analyzed to determine the effects of membrane protein phosphorylation on the connectivity between Photosystem (PS) II centers. Chloroplast membranes which have been incubated in the light with ATP exhibit: (1) a decrease in the variable fluorescence as a function of the initial fluorescence, (2) a shift from a sigmoidal to an exponential fluorescence induction curve, and (3) a reduced amount of the fast (α) component of the induction transient. These phenomenona are completely reversible by dark incubation of the samples (leading to protein dephosphorylation). We conclude that connectivity between PS II centers is reduced as a function of thylakoid membrane protein phosphorylation. This may in turn be the mechanism which increases the amount of absorbed excitation energy available to PS I.

Original languageEnglish (US)
Pages (from-to)336-342
Number of pages7
JournalBBA - Bioenergetics
Volume680
Issue number3
DOIs
StatePublished - Jun 18 1982

Keywords

  • (Chloroplast membrane)
  • Fluorescence
  • Membrane protein phosphorylation
  • Photosystem II
  • Reaction center

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

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