Numbers and functions of plastoquinone molecules associated with photosystem II preparations from Synechococcus sp.

Yuichiro Takahashi, Sakae Katoh

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40 Citations (Scopus)

Abstract

The contents of plastoquinone and PS II electron carriers (QB and Z) of four PS II preparations from the thermophilic cyanobacterium Synechococcus sp. were determined. (1) The oxygen-evolving preparations and the PS II reaction center complexes contained about three and two plastoquinone molecules per PS II, respectively. CP2-b, which represents the functional core of the reaction center complex (Yamagishi, A. and Katoh, S. (1985) Biochim. Biophys. Acta 807, 74-80), had a reduced amount of plastoquinone which is just comparable with the QA content, whereas no plastoquinone was detected in CP2-c, the antenna chlorophyll-protein containing only the 40 kDa subunit. (2) The four preparations were essentially free from vitamin K1. (3) The occurrence of QB and Z in the PS II preparations were determined by measuring oxidation kinetics of Q-A, as well as effects of 3-(3,4-dichlorophenyl)-1,1-dimethylurea, ferricyanide and benzidine on the Q-A oxidation with repetitive flash technique. EPR measurements were also carried out to determine Signal IIs and IIf. QB and Z were present in the oxygen-evolving preparations, while the PS II reaction center complexes had Z, but no or only a residual amount of QB. CP2-b lacked both QB and Z. (4) Q-A was oxidized partly by a back electron transport to Z+ and partly by ferricyanide added in the reaction center complexes. No back reaction between Q-A and P-680+ was detected in CP2-b, which instead showed absorption changes indicative of the triplet formation. It is concluded that three plastoquinone molecules (but not vitamin K1) function as QA, QB and Z and, besides them, there is no extra bound plastoquinone molecule which serves as an additional electron donor or acceptor in the vicinity of the PS II reaction center. The results also suggest that QA, pheophytin and P-680 are located in the interior of the reaction center complexes, but are exposed on removal of the 40 kDa subunit.

Original languageEnglish
Pages (from-to)183-192
Number of pages10
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume848
Issue number2
DOIs
Publication statusPublished - Feb 20 1986
Externally publishedYes

Fingerprint

Plastoquinone
Synechococcus
Photosystem II Protein Complex
Molecules
Vitamin K 1
Pheophytins
Electrons
Diuron
Oxygen
Oxidation
Cyanobacteria
Chlorophyll
Electron Transport
Paramagnetic resonance
Antennas
Kinetics

Keywords

  • (Synechococcus sp.)
  • Electron transport
  • ESR
  • Photosystem II
  • Plastoquinone
  • Signal II

ASJC Scopus subject areas

  • Biophysics

Cite this

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title = "Numbers and functions of plastoquinone molecules associated with photosystem II preparations from Synechococcus sp.",
abstract = "The contents of plastoquinone and PS II electron carriers (QB and Z) of four PS II preparations from the thermophilic cyanobacterium Synechococcus sp. were determined. (1) The oxygen-evolving preparations and the PS II reaction center complexes contained about three and two plastoquinone molecules per PS II, respectively. CP2-b, which represents the functional core of the reaction center complex (Yamagishi, A. and Katoh, S. (1985) Biochim. Biophys. Acta 807, 74-80), had a reduced amount of plastoquinone which is just comparable with the QA content, whereas no plastoquinone was detected in CP2-c, the antenna chlorophyll-protein containing only the 40 kDa subunit. (2) The four preparations were essentially free from vitamin K1. (3) The occurrence of QB and Z in the PS II preparations were determined by measuring oxidation kinetics of Q-A, as well as effects of 3-(3,4-dichlorophenyl)-1,1-dimethylurea, ferricyanide and benzidine on the Q-A oxidation with repetitive flash technique. EPR measurements were also carried out to determine Signal IIs and IIf. QB and Z were present in the oxygen-evolving preparations, while the PS II reaction center complexes had Z, but no or only a residual amount of QB. CP2-b lacked both QB and Z. (4) Q-A was oxidized partly by a back electron transport to Z+ and partly by ferricyanide added in the reaction center complexes. No back reaction between Q-A and P-680+ was detected in CP2-b, which instead showed absorption changes indicative of the triplet formation. It is concluded that three plastoquinone molecules (but not vitamin K1) function as QA, QB and Z and, besides them, there is no extra bound plastoquinone molecule which serves as an additional electron donor or acceptor in the vicinity of the PS II reaction center. The results also suggest that QA, pheophytin and P-680 are located in the interior of the reaction center complexes, but are exposed on removal of the 40 kDa subunit.",
keywords = "(Synechococcus sp.), Electron transport, ESR, Photosystem II, Plastoquinone, Signal II",
author = "Yuichiro Takahashi and Sakae Katoh",
year = "1986",
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T1 - Numbers and functions of plastoquinone molecules associated with photosystem II preparations from Synechococcus sp.

AU - Takahashi, Yuichiro

AU - Katoh, Sakae

PY - 1986/2/20

Y1 - 1986/2/20

N2 - The contents of plastoquinone and PS II electron carriers (QB and Z) of four PS II preparations from the thermophilic cyanobacterium Synechococcus sp. were determined. (1) The oxygen-evolving preparations and the PS II reaction center complexes contained about three and two plastoquinone molecules per PS II, respectively. CP2-b, which represents the functional core of the reaction center complex (Yamagishi, A. and Katoh, S. (1985) Biochim. Biophys. Acta 807, 74-80), had a reduced amount of plastoquinone which is just comparable with the QA content, whereas no plastoquinone was detected in CP2-c, the antenna chlorophyll-protein containing only the 40 kDa subunit. (2) The four preparations were essentially free from vitamin K1. (3) The occurrence of QB and Z in the PS II preparations were determined by measuring oxidation kinetics of Q-A, as well as effects of 3-(3,4-dichlorophenyl)-1,1-dimethylurea, ferricyanide and benzidine on the Q-A oxidation with repetitive flash technique. EPR measurements were also carried out to determine Signal IIs and IIf. QB and Z were present in the oxygen-evolving preparations, while the PS II reaction center complexes had Z, but no or only a residual amount of QB. CP2-b lacked both QB and Z. (4) Q-A was oxidized partly by a back electron transport to Z+ and partly by ferricyanide added in the reaction center complexes. No back reaction between Q-A and P-680+ was detected in CP2-b, which instead showed absorption changes indicative of the triplet formation. It is concluded that three plastoquinone molecules (but not vitamin K1) function as QA, QB and Z and, besides them, there is no extra bound plastoquinone molecule which serves as an additional electron donor or acceptor in the vicinity of the PS II reaction center. The results also suggest that QA, pheophytin and P-680 are located in the interior of the reaction center complexes, but are exposed on removal of the 40 kDa subunit.

AB - The contents of plastoquinone and PS II electron carriers (QB and Z) of four PS II preparations from the thermophilic cyanobacterium Synechococcus sp. were determined. (1) The oxygen-evolving preparations and the PS II reaction center complexes contained about three and two plastoquinone molecules per PS II, respectively. CP2-b, which represents the functional core of the reaction center complex (Yamagishi, A. and Katoh, S. (1985) Biochim. Biophys. Acta 807, 74-80), had a reduced amount of plastoquinone which is just comparable with the QA content, whereas no plastoquinone was detected in CP2-c, the antenna chlorophyll-protein containing only the 40 kDa subunit. (2) The four preparations were essentially free from vitamin K1. (3) The occurrence of QB and Z in the PS II preparations were determined by measuring oxidation kinetics of Q-A, as well as effects of 3-(3,4-dichlorophenyl)-1,1-dimethylurea, ferricyanide and benzidine on the Q-A oxidation with repetitive flash technique. EPR measurements were also carried out to determine Signal IIs and IIf. QB and Z were present in the oxygen-evolving preparations, while the PS II reaction center complexes had Z, but no or only a residual amount of QB. CP2-b lacked both QB and Z. (4) Q-A was oxidized partly by a back electron transport to Z+ and partly by ferricyanide added in the reaction center complexes. No back reaction between Q-A and P-680+ was detected in CP2-b, which instead showed absorption changes indicative of the triplet formation. It is concluded that three plastoquinone molecules (but not vitamin K1) function as QA, QB and Z and, besides them, there is no extra bound plastoquinone molecule which serves as an additional electron donor or acceptor in the vicinity of the PS II reaction center. The results also suggest that QA, pheophytin and P-680 are located in the interior of the reaction center complexes, but are exposed on removal of the 40 kDa subunit.

KW - (Synechococcus sp.)

KW - Electron transport

KW - ESR

KW - Photosystem II

KW - Plastoquinone

KW - Signal II

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U2 - 10.1016/0005-2728(86)90040-X

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