Redox reactions on the reducing side of photosystem II in chloroplasts with altered herbicide binding properties

Jane Bowes, A. R. Crofts, C. J. Arntzen

Research output: Contribution to journalArticlepeer-review

96 Scopus citations

Abstract

Measurements of chlorophyll fluorescence have been used to monitor electron transfer from Q (the primary electron acceptor of photosystem II) to B (the bound quinone which serves as the secondary acceptor) in chloroplasts isolated from atrazine-susceptible and atrazine-resistant pigweed chloroplasts. The Q- → B electron transfer was at least 10-fold slower in the plastids from resistant plants. Binary oscillations in the rate of Q- decay after a series of flashes were of opposite phase in the two types. The data are interpreted to indicate that the apoprotein of B is altered in the photosytem II complex of the two types of plants-this is correlated to altered binding affinity of herbicides to this component and may be related to altered redox properties of the bound quinone cofactor.

Original languageEnglish (US)
Pages (from-to)303-308
Number of pages6
JournalArchives of Biochemistry and Biophysics
Volume200
Issue number1
DOIs
StatePublished - Mar 1980

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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