Fluorescence lifetime studies of cyanobacterial photosystem II mutants

Edith Bittersmann, Willem Vermaas

Research output: Contribution to journalArticle

46 Citations (Scopus)

Abstract

Time-resolved and steady-state fluorescence spectra have been determined in intact cells of wild type and selected Photosystem II mutants of the cyanobacterium Synechocystis sp. PCC 6803. Upon excitation of phycobilisome components, in wild type fluorescence lifetimes and spectra are observed that are compatible with energy transfer within the phycobilisome, between the phycobilisome and Photosystem II, and within Photosystem II (PS II). In a mutant carrying a spinach/Synechocystis CP47 hybrid protein (one of the chlorophyll-binding antennae within PS II), energy transfer between phycobilisomes and PS II. In a mutant containing some CP43 (another chlorophyll-binding antenna protein in PS II) but lacking all other major PS II proteins, chlorophyll can still be bound to CP43, but significant long-lived fluorescence from this chlorophyll could not be observed. In a mutant lacking all major PS II components, phycobilisomes displayed a fluorescence yield larger than in wild type, but considerably smaller than observed in isolated systems. The conformation of one or more phycobilins in or near the anchor protein most likely is important in determining the fluorescence yield of phycobilisomes.

Original languageEnglish (US)
Pages (from-to)105-116
Number of pages12
JournalBBA - Bioenergetics
Volume1098
Issue number1
DOIs
StatePublished - Dec 3 1991

Fingerprint

Photosystem II Protein Complex
Phycobilisomes
Fluorescence
Chlorophyll
Chlorophyll Binding Proteins
Synechocystis
Energy Transfer
Energy transfer
Phycobilins
Proteins
Antennas
Spinacia oleracea
Cyanobacteria
Anchors
Conformations

Keywords

  • Chlorophyll fluorescence
  • Cyanobacterium
  • Energy transfer
  • Photosystem II
  • Phycobilisome

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Molecular Biology
  • Biochemistry

Cite this

Fluorescence lifetime studies of cyanobacterial photosystem II mutants. / Bittersmann, Edith; Vermaas, Willem.

In: BBA - Bioenergetics, Vol. 1098, No. 1, 03.12.1991, p. 105-116.

Research output: Contribution to journalArticle

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AB - Time-resolved and steady-state fluorescence spectra have been determined in intact cells of wild type and selected Photosystem II mutants of the cyanobacterium Synechocystis sp. PCC 6803. Upon excitation of phycobilisome components, in wild type fluorescence lifetimes and spectra are observed that are compatible with energy transfer within the phycobilisome, between the phycobilisome and Photosystem II, and within Photosystem II (PS II). In a mutant carrying a spinach/Synechocystis CP47 hybrid protein (one of the chlorophyll-binding antennae within PS II), energy transfer between phycobilisomes and PS II. In a mutant containing some CP43 (another chlorophyll-binding antenna protein in PS II) but lacking all other major PS II proteins, chlorophyll can still be bound to CP43, but significant long-lived fluorescence from this chlorophyll could not be observed. In a mutant lacking all major PS II components, phycobilisomes displayed a fluorescence yield larger than in wild type, but considerably smaller than observed in isolated systems. The conformation of one or more phycobilins in or near the anchor protein most likely is important in determining the fluorescence yield of phycobilisomes.

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