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

Naoto Yamaguchi, Yuichiro Takahashi, Kimiyuki Satoh

Research output: Contribution to journalArticle

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 1988

Fingerprint

Photosystem II
Photosystem II Protein Complex
Polypeptides
Chlorophyll
Chlorophyll Binding Proteins
photosystem II
digitonin
Isolation
Digitonin
polypeptides
chlorophyll
thiocyanates
Electron Transport
Proteins
electron
Peptides
electron transfer
Potassium
Diphenylcarbazide
Pheophytins

Keywords

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

ASJC Scopus subject areas

  • Statistics, Probability and Uncertainty
  • Applied Mathematics
  • Ecology
  • Cell Biology
  • Physiology
  • Plant Science

Cite this

Isolation and characterization of a photosystem II core complex depleted in the 43 kDa-chlorophyll-binding subunit. / Yamaguchi, Naoto; Takahashi, Yuichiro; Satoh, Kimiyuki.

In: Plant and Cell Physiology, Vol. 29, No. 1, 01.1988, p. 123-129.

Research output: Contribution to journalArticle

@article{ed43fdb61a63419e9aa1e23dcedd7067,
title = "Isolation and characterization of a photosystem II core complex depleted in the 43 kDa-chlorophyll-binding subunit",
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",
keywords = "Chlorophyll protein, Photosynthesis, Photosystem II, Potassium thiocyanate, Reaction center",
author = "Naoto Yamaguchi and Yuichiro Takahashi and Kimiyuki Satoh",
year = "1988",
month = "1",
language = "English",
volume = "29",
pages = "123--129",
journal = "Plant and Cell Physiology",
issn = "0032-0781",
publisher = "Oxford University Press",
number = "1",

}

TY - JOUR

T1 - Isolation and characterization of a photosystem II core complex depleted in the 43 kDa-chlorophyll-binding subunit

AU - Yamaguchi, Naoto

AU - Takahashi, Yuichiro

AU - Satoh, Kimiyuki

PY - 1988/1

Y1 - 1988/1

N2 - 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

AB - 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

KW - Chlorophyll protein

KW - Photosynthesis

KW - Photosystem II

KW - Potassium thiocyanate

KW - Reaction center

UR - http://www.scopus.com/inward/record.url?scp=0000029528&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0000029528&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:0000029528

VL - 29

SP - 123

EP - 129

JO - Plant and Cell Physiology

JF - Plant and Cell Physiology

SN - 0032-0781

IS - 1

ER -