Results 281 to 290 of about 122,048 (323)
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Photosystem II activity and pigment-protein complexes in flashed bean leaves
Plant Science Letters, 1973Abstract Bean leaves exposed to cycles of 2 min light—118 min dark, (1) can photoreduce cytochrome f ; (2) have cytochrome b -559 HP ; (3) have a DCMU (3-[3′,4′-dichlorophenyl]-1,1-dimethylurea)-sensitive Hill reaction. Detergent extracts of the plastids show only pigment-protein complex I.
R.G Hiller, Dori Pilger, Sandra Genge
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Langmuir, 2016
The development of artificial photosynthesis has focused on the efficient coupling of reaction at photoanode and cathode, wherein the production of hydrogen (or energy carriers) is coupled to the electrons derived from water-splitting reactions. The natural photosystem II (PSII) complex splits water efficiently using light energy. The PSII complex is a
Tomoyasu, Noji +7 more
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The development of artificial photosynthesis has focused on the efficient coupling of reaction at photoanode and cathode, wherein the production of hydrogen (or energy carriers) is coupled to the electrons derived from water-splitting reactions. The natural photosystem II (PSII) complex splits water efficiently using light energy. The PSII complex is a
Tomoyasu, Noji +7 more
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1998
The enzymes responsible for reversible phosphorylation of components of photosynthetic complexes are presumed to be associated with the thylakoid membrane. Evidence supporting the presence of multiple protein kinases in this system is mounting. Phosphorylation appears to be redox-regulated with activity favoured by reducing conditions.
Helen L. Race +3 more
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The enzymes responsible for reversible phosphorylation of components of photosynthetic complexes are presumed to be associated with the thylakoid membrane. Evidence supporting the presence of multiple protein kinases in this system is mounting. Phosphorylation appears to be redox-regulated with activity favoured by reducing conditions.
Helen L. Race +3 more
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Multiple copies of the PsbQ protein in a cyanobacterial photosystem II assembly intermediate complex
Photosynthesis Research, 2015Photosystem II (PSII) undergoes frequent damage owing to the demanding electron transfer chemistry it performs. To sustain photosynthetic activity, damaged PSII undergoes a complex repair cycle consisting of many transient intermediate complexes. By purifying PSII from the cyanobacterium Synechocystis sp.
Haijun, Liu +2 more
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Co-translational Assembly of the D1 Protein into Photosystem II Complexes
1998Chloroplast-encoded D1 and D2 proteins, the heterodimer reaction centre polypeptides of photosystem II (PS II) bind all the components necessary for the primary charge separation. The D1 protein has an unusually high turnover rate as compared to the other chloroplast proteins (1,2).
Lixin Zhang +3 more
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Biochemistry, 1993
The chlorophyll-protein complexes that form the antenna system of photosystem II have been purified and analyzed in terms of the commonly observed chlorophyll spectral forms. With the exception of chlorophyll b, which is known to be associated with the complexes comprising the outer antenna (LHCII, CP24, CP26, CP29), the spectral forms occur with ...
JENNINGS RC +4 more
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The chlorophyll-protein complexes that form the antenna system of photosystem II have been purified and analyzed in terms of the commonly observed chlorophyll spectral forms. With the exception of chlorophyll b, which is known to be associated with the complexes comprising the outer antenna (LHCII, CP24, CP26, CP29), the spectral forms occur with ...
JENNINGS RC +4 more
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ELECTROPHORESIS, 1996
AbstractThe electrophoretic migration behavior of three closely related hydrophobic intrinsic membrane proteins of the photosystem II light‐harvesting complex (LHC II) was investigated in free solution capillary electrophoresis at pH 8.0–10 with running electrolyte solutions containing either anionic, zwitterionic or nonionic detergents.
Zolla L +4 more
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AbstractThe electrophoretic migration behavior of three closely related hydrophobic intrinsic membrane proteins of the photosystem II light‐harvesting complex (LHC II) was investigated in free solution capillary electrophoresis at pH 8.0–10 with running electrolyte solutions containing either anionic, zwitterionic or nonionic detergents.
Zolla L +4 more
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Plant Physiology and Biochemistry, 2005
The stability of chlorophyll-protein complexes of photosystem I (PSI) and photosystem II (PSII) was investigated by chlorophyll (Chl) fluorescence spectroscopy, absorption spectra and native green gel separation system during flag leaf senescence of two rice varieties (IIyou 129 and Shanyou 63) grown under outdoor conditions.
Yunlai, Tang +2 more
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The stability of chlorophyll-protein complexes of photosystem I (PSI) and photosystem II (PSII) was investigated by chlorophyll (Chl) fluorescence spectroscopy, absorption spectra and native green gel separation system during flag leaf senescence of two rice varieties (IIyou 129 and Shanyou 63) grown under outdoor conditions.
Yunlai, Tang +2 more
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Photosynthesis Research, 1990
Chloride plays a key role in activating the photosynethetic oxygen-evolving complex (OEC) of Photosystem II, but the OEC is only one of many enzymes affected by this anion. Some of the mechanistic features of Cl(-) involvement in water-splitting resemble those of other proteins whose structure and chemistry are known in detail.
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Chloride plays a key role in activating the photosynethetic oxygen-evolving complex (OEC) of Photosystem II, but the OEC is only one of many enzymes affected by this anion. Some of the mechanistic features of Cl(-) involvement in water-splitting resemble those of other proteins whose structure and chemistry are known in detail.
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Journal of Protein Chemistry, 2001
Changes in the protein secondary structure and electron transport activity of the Triton X-100-treated photosystem I (PSI) and photosystem II (PSII) complexes after strong illumination treatment were studied using Fourier transform-infrared (FT-IR) spectroscopy and an oxygen electrode. Short periods of photoinhibitory treatment led to obvious decreases
X, Ruan +7 more
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Changes in the protein secondary structure and electron transport activity of the Triton X-100-treated photosystem I (PSI) and photosystem II (PSII) complexes after strong illumination treatment were studied using Fourier transform-infrared (FT-IR) spectroscopy and an oxygen electrode. Short periods of photoinhibitory treatment led to obvious decreases
X, Ruan +7 more
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