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פותח על ידי קלירמאש פתרונות בע"מ -
Isolation and spectroscopic characterization of a plantlike photosystem II reaction center from the cyanobacterium Synechocystis sp. 6803
Year:
1995
Source of publication :
Biochemistry (source )
Authors :
אורן-שמיר, מיכל
;
.
Volume :
34
Co-Authors:
Oren-Shamir, M., Department of Biochemistry, Weizmann Institute of Science, Rehovot, 76100, Israel, Department of Plant Genetics, Weizmann Institute of Science, Rehovot, 76100, Israel, Department of Ornamental Horticulture, Agricultural Research Organization, Volcani Center, P.O.B. 6, Bet Dagan, 50250, Israel
Sai, P.S.M., Department of Biochemistry, Weizmann Institute of Science, Rehovot, 76100, Israel
Edelman, M., Department of Plant Genetics, Weizmann Institute of Science, Rehovot, 76100, Israel
Scherz, A., Department of Biochemistry, Weizmann Institute of Science, Rehovot, 76100, Israel
Facilitators :
From page:
5523
To page:
5526
(
Total pages:
4
)
Abstract:
A chlorophyll-protein complex has been isolated from the cyanobacterium Synechocystis sp. PCC 6803 that closely resembles higher plant photosystem II reaction centers in spectral properties. The Synechocystis complex has a pigment content of 5-7 chlorophyll a molecules:1 Cyt b559:2 pheophytins; an optical absorption redmost transition at ∼675 nm; and a nonconservative circular dichroism red signal, with extrema at 682 (+) and 652 (-) nm. Upon illumination, the Synechocystis D1/D2/Cyt b559 complex accumulates reduced pheophytin. LDS-PAGE and/or immunoblotting showed the D1, D2, and Cyt b559 proteins, aggregated and degraded forms of D1 and possibly D2, and traces of ATP synthase and the CP47 photosystem II chlorophyll protein. The availability of such a Synechocystis preparation opens the way for employing site-directed mutagenesis in studying primary reactions of oxygenic photosynthesis. © 1995 American Chemical Society.
Note:
Related Files :
chlorophyll
circular dichroism
Electrophoresis, Polyacrylamide Gel
pheophytin
photosynthesis
spectroscopy
עוד תגיות
תוכן קשור
More details
DOI :
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
32109
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 01:07
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Scientific Publication
Isolation and spectroscopic characterization of a plantlike photosystem II reaction center from the cyanobacterium Synechocystis sp. 6803
34
Oren-Shamir, M., Department of Biochemistry, Weizmann Institute of Science, Rehovot, 76100, Israel, Department of Plant Genetics, Weizmann Institute of Science, Rehovot, 76100, Israel, Department of Ornamental Horticulture, Agricultural Research Organization, Volcani Center, P.O.B. 6, Bet Dagan, 50250, Israel
Sai, P.S.M., Department of Biochemistry, Weizmann Institute of Science, Rehovot, 76100, Israel
Edelman, M., Department of Plant Genetics, Weizmann Institute of Science, Rehovot, 76100, Israel
Scherz, A., Department of Biochemistry, Weizmann Institute of Science, Rehovot, 76100, Israel
Isolation and spectroscopic characterization of a plantlike photosystem II reaction center from the cyanobacterium Synechocystis sp. 6803
A chlorophyll-protein complex has been isolated from the cyanobacterium Synechocystis sp. PCC 6803 that closely resembles higher plant photosystem II reaction centers in spectral properties. The Synechocystis complex has a pigment content of 5-7 chlorophyll a molecules:1 Cyt b559:2 pheophytins; an optical absorption redmost transition at ∼675 nm; and a nonconservative circular dichroism red signal, with extrema at 682 (+) and 652 (-) nm. Upon illumination, the Synechocystis D1/D2/Cyt b559 complex accumulates reduced pheophytin. LDS-PAGE and/or immunoblotting showed the D1, D2, and Cyt b559 proteins, aggregated and degraded forms of D1 and possibly D2, and traces of ATP synthase and the CP47 photosystem II chlorophyll protein. The availability of such a Synechocystis preparation opens the way for employing site-directed mutagenesis in studying primary reactions of oxygenic photosynthesis. © 1995 American Chemical Society.
Scientific Publication
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