Isolation and characterization of a photosystem II core complex depleted in the 43 kDa-chlorophyll-binding subunit

Naoto Yamaguchi, Yuichiro Takahashi, Kimiyuki Satoh

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26 Citations (Scopus)

Abstract

The photosystem II core complex purified from digitonin extracts of spinach chloroplasts was resolved into two chlorophyll-protein complexes by digitonin polyacrylamide gel electrophoresis after treatment with 1 M potassium thiocyanate. One of the chlorophyll-protein complexes resolved consisted of 47, 32, 30 and 9 kDa polypeptides and the other was complementally composed of only the 43 kDa polypeptide. The former complex was highly active in the photoreduction of 2, 6-dichlorophenol indophenol by 1,5-diphenylcarbazide and retained all of the components responsible for the electron transport from the secondary electron donor (Z) to the primary electron acceptor (QA). EPR signal IIfast and IIslow were also preserved in this complex although their hyperfine structures were largely modified. The complex was estimated to contain 1.8 molecules of plastoquinone A as well as 1.5, 3.7 and 3.9 molecules of cytochrome b559, pheophytin α and β-carotene, respectively, per QA. These results indicate that potassium thiocyanate specifically removes the 43 kDa polypeptide from the PS II core complex leaving the electron transport system in an almost intact state. Copyring

Original languageEnglish
Pages (from-to)123-129
Number of pages7
JournalPlant and Cell Physiology
Volume29
Issue number1
Publication statusPublished - Jan 1 1988

Keywords

  • Chlorophyll protein
  • Photosynthesis
  • Photosystem II
  • Potassium thiocyanate
  • Reaction center

ASJC Scopus subject areas

  • Physiology
  • Plant Science
  • Cell Biology

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