Results 1 to 10 of about 21,134 (164)

Truncated recombinant light harvesting complex II proteins are substrates for a protein kinase associated with photosystem II core complexes [PDF]

open access: yesFEBS Letters, 1998
Previous studies directed towards understanding phosphorylation of the chlorophyll a/b binding proteins comprising light harvesting complex II (LHC II) have concentrated on a single phosphorylation site located close to the N‐terminus of the mature proteins.
John Allen, Harald Paulsen
exaly   +3 more sources

Tomato B cell receptor-associated protein 31 homologs enhance thermotolerance by promoting chloroplast PSBW accumulation and stabilizing the PSII–LHCII complex [PDF]

open access: yesPlant Communications
B-cell receptor-associated protein 31 (BAP31) is an endoplasmic reticulum (ER) transmembrane protein in humans that regulates protein trafficking, apoptosis, and inflammatory responses to maintain cellular homeostasis. However, its role in plants remains
Chong Chen   +10 more
doaj   +2 more sources

Light-induced degradation of D2 protein in isolated photosystem II reaction center complex [PDF]

open access: yesFEBS Letters, 1992
When isolated photosystem II reaction centers from spinach are exposed to photoinhibitory light in the presence of an electron acceptor, breakdown products of the D2 protein at 28, 25, 23, 18, 9, 5 and 4.5 kDa are detected by immunoblotting with a monospecific anti‐D2 polyclonal antibody.
Patrizia Polverino De Laureto   +2 more
exaly   +5 more sources

Advances in the Understanding of the Lifecycle of Photosystem II

open access: yesMicroorganisms, 2022
Photosystem II is a light-driven water-plastoquinone oxidoreductase present in cyanobacteria, algae and plants. It produces molecular oxygen and protons to drive ATP synthesis, fueling life on Earth.
Virginia M. Johnson, Himadri B. Pakrasi
doaj   +1 more source

Quality control of photosystem II: lipid peroxidation accelerates photoinhibition under excessive illumination. [PDF]

open access: yesPLoS ONE, 2012
Environmental stresses lower the efficiency of photosynthesis and sometimes cause irreversible damage to plant functions. When spinach thylakoids and Photosystem II membranes were illuminated with excessive visible light (100-1,000 µmol photons m(-1) s ...
Tiffanie Chan   +17 more
doaj   +1 more source

A novel chlorophyll protein complex in the repair cycle of photosystem II [PDF]

open access: yesProceedings of the National Academy of Sciences, 2019
In oxygenic photosynthetic organisms, photosystem II (PSII) is a unique membrane protein complex that catalyzes light-driven oxidation of water. PSII undergoes frequent damage due to its demanding photochemistry. It must undergo a repair and reassembly process following photodamage, many facets of which remain unknown.
Daniel A. Weisz   +9 more
openaire   +2 more sources

Photosynthetic Light Harvesting and Thylakoid Organization in a CRISPR/Cas9 Arabidopsis Thaliana LHCB1 Knockout Mutant

open access: yesFrontiers in Plant Science, 2022
Light absorbed by chlorophylls of Photosystems II and I drives oxygenic photosynthesis. Light-harvesting complexes increase the absorption cross-section of these photosystems.
Hamed Sattari Vayghan   +10 more
doaj   +1 more source

Dynamics of photosystem II: a proteomic approach to thylakoid protein complexes [PDF]

open access: yesJournal of Experimental Botany, 2004
Oxygenic photosynthesis produces various radicals and active oxygen species with harmful effects on photosystem II (PSII). Such photodamage occurs at all light intensities. Damaged PSII centres, however, do not usually accumulate in the thylakoid membrane due to a rapid and efficient repair mechanism.
E-M, Aro   +7 more
openaire   +2 more sources

Evidence for a chlorophylla/b—protein complex associated with Photosystem II [PDF]

open access: yesFEBS Letters, 1984
A new chlorophylla/b—protein complex designated as LHCPx was separated by SDS—PAGE. This complex differs from the light‐harvesting chla/b—protein of PS II, by its chla/bratio, its fluorescence properties and its apoprotein composition. Evidence is provided that this complex corresponds to a part of PS I antenna.
Remy, R., Ambard-Bretteville, F.
openaire   +1 more source

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