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פותח על ידי קלירמאש פתרונות בע"מ -
Separate photosensitizers mediate degradation of the 32-kDa photosystem II reaction center protein in the visible and UV spectral regions.
Year:
1989
Authors :
גאבה, ויקטור
;
.
Volume :
86
Co-Authors:
Greenberg, B.M., Department of Plant Genetics, Weizmann Institute of Science, Rehovot, Israel.
Gaba, V., Department of Plant Genetics, Weizmann Institute of Science, Rehovot, Israel.
Canaani, O., Department of Plant Genetics, Weizmann Institute of Science, Rehovot, Israel.
Malkin, S., Department of Plant Genetics, Weizmann Institute of Science, Rehovot, Israel.
Mattoo, A.K., Department of Plant Genetics, Weizmann Institute of Science, Rehovot, Israel.
Edelman, M., Department of Plant Genetics, Weizmann Institute of Science, Rehovot, Israel.
Facilitators :
From page:
6617
To page:
6620
(
Total pages:
4
)
Abstract:
A component of the photosystem II reaction center, the 32-kDa protein, is rapidly turned over in the light. The mechanism of its light-dependent metabolism is largely unknown. We quantified the rate of 32-kDa protein degradation over a broad spectral range (UV, visible, and far red). The quantum yield for degradation was highest in the UVB (280-320 nm) region. Spectral evidence demonstrates two distinctly different photosensitizers for 32-kDa protein degradation. The data implicate the bulk photosynthetic pigments (primarily chlorophyll) in the visible and far red regions, and plastoquinone (in one or more of its redox states) in the UV region. A significant portion of 32-kDa protein degradation in sunlight is attributed to UVB irradiance.
Note:
Related Files :
chlorophyll
light
metabolism
photosynthesis
Plants
ultraviolet radiation
עוד תגיות
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More details
DOI :
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
19899
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:32
Scientific Publication
Separate photosensitizers mediate degradation of the 32-kDa photosystem II reaction center protein in the visible and UV spectral regions.
86
Greenberg, B.M., Department of Plant Genetics, Weizmann Institute of Science, Rehovot, Israel.
Gaba, V., Department of Plant Genetics, Weizmann Institute of Science, Rehovot, Israel.
Canaani, O., Department of Plant Genetics, Weizmann Institute of Science, Rehovot, Israel.
Malkin, S., Department of Plant Genetics, Weizmann Institute of Science, Rehovot, Israel.
Mattoo, A.K., Department of Plant Genetics, Weizmann Institute of Science, Rehovot, Israel.
Edelman, M., Department of Plant Genetics, Weizmann Institute of Science, Rehovot, Israel.
Separate photosensitizers mediate degradation of the 32-kDa photosystem II reaction center protein in the visible and UV spectral regions.
A component of the photosystem II reaction center, the 32-kDa protein, is rapidly turned over in the light. The mechanism of its light-dependent metabolism is largely unknown. We quantified the rate of 32-kDa protein degradation over a broad spectral range (UV, visible, and far red). The quantum yield for degradation was highest in the UVB (280-320 nm) region. Spectral evidence demonstrates two distinctly different photosensitizers for 32-kDa protein degradation. The data implicate the bulk photosynthetic pigments (primarily chlorophyll) in the visible and far red regions, and plastoquinone (in one or more of its redox states) in the UV region. A significant portion of 32-kDa protein degradation in sunlight is attributed to UVB irradiance.
Scientific Publication
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