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 language | English |
|---|---|
| Pages (from-to) | 183-192 |
| Number of pages | 10 |
| Journal | Biochimica et Biophysica Acta - Bioenergetics |
| Volume | 848 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Feb 20 1986 |
| Externally published | Yes |
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Keywords
- (Synechococcus sp.)
- Electron transport
- ESR
- Photosystem II
- Plastoquinone
- Signal II
ASJC Scopus subject areas
- Biophysics
Cite this
Numbers and functions of plastoquinone molecules associated with photosystem II preparations from Synechococcus sp. / Takahashi, Yuichiro; Katoh, Sakae.
In: Biochimica et Biophysica Acta - Bioenergetics, Vol. 848, No. 2, 20.02.1986, p. 183-192.Research output: Contribution to journal › Article
}
TY - JOUR
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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UR - http://www.scopus.com/inward/citedby.url?scp=0022571930&partnerID=8YFLogxK
U2 - 10.1016/0005-2728(86)90040-X
DO - 10.1016/0005-2728(86)90040-X
M3 - Article
VL - 848
SP - 183
EP - 192
JO - Biochimica et Biophysica Acta - Bioenergetics
JF - Biochimica et Biophysica Acta - Bioenergetics
SN - 0005-2728
IS - 2
ER -