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The redox state of the plastoquinone pool controls the level of the light-harvesting chlorophyll a/b binding protein complex II (LHC II) during photoacclimation

Autor: D H, Yang, B, Andersson, E M, Aro, I, Ohad

Publikováno v: Photosynthesis research. 68(2)

A cytochrome b (6) f deficient mutant of Lemna perpusilla maintains a constant and lower level of the light-harvesting chl a/b-binding protein complex II (LHC II) as compared to the wild type plants at low-light intensities. Inhibition of the plastoq

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4c478038946245c873a907f03b376828
https://pubmed.ncbi.nlm.nih.gov/16228339

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Inhibition of Photosystem II activity by saturating single turnover flashes in calcium-depleted and active Photosystem II

Autor: N, Keren, I, Ohad, A W, Rutherford, F, Drepper, A, Krieger-Liszkay

Publikováno v: Photosynthesis research. 63(3)

Inhibition of Photosystem II (PS II) activity induced by continuous light or by saturating single turnover flashes was investigated in Ca(2+)-depleted, Mn-depleted and active PS II enriched membrane fragments. While Ca(2+)- and Mn-depleted PS II were

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b2d3e816a10dbe64f32865d326b0fb12
https://pubmed.ncbi.nlm.nih.gov/16228431

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Regulation of Photosystem II core protein phosphorylation at the substrate level: Light induces exposure of the CP43 chlorophyll a protein complex to thylakoid protein kinase(s)

Autor: M, Vink, H, Zer, R G, Herrmann, B, Andersson, I, Ohad

Publikováno v: Photosynthesis research. 64(2-3)

Light induces conformational changes in the CP43 chl-a-protein antenna complex in isolated PS II core-complexes exposing phosphorylation site(s) to PS II core-associated protein kinase(s), to added solubilized thylakoid protein kinase(s), as well as

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5112786c1818cf6dfec1b29796117c20
https://pubmed.ncbi.nlm.nih.gov/16228459

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Passive entry of CO2 and its energy-dependent intracellular conversion to HCO3- in cyanobacteria are driven by a photosystem I-generated deltamuH+

Autor: D, Tchernov, Y, Helman, N, Keren, B, Luz, I, Ohad, L, Reinhold, T, Ogawa, A, Kaplan

Publikováno v: The Journal of biological chemistry. 276(26)

CO(2) entry into Synechococcus sp. PCC7942 cells was drastically inhibited by the water channel blocker p-chloromercuriphenylsulfonic acid suggesting that CO(2) uptake is, for the most part, passive via aquaporins with subsequent energy-dependent con

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::17e76ff10b9d1ff149c33224a8d8abba
https://pubmed.ncbi.nlm.nih.gov/11297562

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Activation/deactivation cycle of redox-controlled thylakoid protein phosphorylation. Role of plastoquinol bound to the reduced cytochrome bf complex

Autor: A V, Vener, P J, Van Kan, A, Gal, B, Andersson, I, Ohad

Publikováno v: The Journal of biological chemistry. 270(42)

Signal transduction via light-dependent redox control of reversible thylakoid protein phosphorylation has evolved in plants as a unique mechanism for controlling events related to light energy utilization. Here we report for the first time that prote

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e5c4bc746353c9713f801d210be4ea0c
https://pubmed.ncbi.nlm.nih.gov/7559660

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Photoinactivation of photosystem II induces changes in the photochemical reaction center II abolishing the regulatory role of the QB site in the D1 protein degradation

Autor: H, Zer, I, Ohad

Publikováno v: European journal of biochemistry. 231(2)

The effect of 3-(3,4-dichlorophenyl)-1,1-dimethyl urea (diuron) binding at the secondary quinone (QB) binding site of reaction center II (RCII), on the high-light-induced degradation of the RCII proteins D1 and D2, and the core proteins CP43 and CP47

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::aad21f25fa9721f1db166a2277c8d4a2
https://pubmed.ncbi.nlm.nih.gov/7635157

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Oscillations of reaction center II-D1 protein degradation in vivo induced by repetitive light flashes. Correlation between the level of RCII-QB- and protein degradation in low light

Autor: N, Keren, H, Gong, I, Ohad

Publikováno v: The Journal of biological chemistry. 270(2)

The D1 protein subunit of the photochemical reaction center II (RCII) turns over rapidly in oxygenic photosynthetic organisms exposed to the light. At high photon flux densities (PFD), photoinactivation of RCII precedes the degradation of the D1 prot

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1de9f39a29f8e64a4f1a9dd48bd93a78
https://pubmed.ncbi.nlm.nih.gov/7822315

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