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- Suorsa, Marjaana, et al.
(författare)
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Dark-adapted spinach thylakoid protein heterogeneity offers insights into the photosystem II repair cycle
- 2014
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Ingår i: Biochimica et Biophysica Acta - Bioenergetics. - : Elsevier BV. - 0005-2728 .- 1879-2650. ; 1837:9, s. 1463-1471
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Tidskriftsartikel (refereegranskat)abstract
- In higher plants, thylakoid membrane protein complexes show lateral heterogeneity in their distribution: photosystem (PS) II complexes are mostly located in grana stacks, whereas PSI and adenosine triphosphate (ATP) synthase are mostly found in the stroma-exposed thylakoids. However, recent research has revealed strong dynamics in distribution of photosystems and their light harvesting antenna along the thylakoid membrane. Here, the dark-adapted spinach (Spinacia oleracea L.) thylakoid network was mechanically fragmented and the composition of distinct PSII-related proteins in various thylakoid subdomains was analyzed in order to get more insights into the composition and localization of various PSII subcomplexes and auxiliary proteins during the PSII repair cycle. Most of the PSII subunits followed rather equal distribution with roughly 70% of the proteins located collectively in the grana thylakoids and grana margins; however, the low molecular mass subunits PsbW and PsbX as well as the PsbS proteins were found to be more exclusively located in grana thylakoids. The auxiliary proteins assisting in repair cycle of PSII were mostly located in stroma-exposed thylakoids, with the exception of THYLAKOID LUMEN PROTEIN OF 18.3 (TLP18.3), which was more evenly distributed between the grana and stroma thylakoids. The TL29 protein was present exclusively in grana thylakoids. Intriguingly, PROTON GRADIENT REGULATIONS (PGR5) was found to be distributed quite evenly between grana and stroma thylakoids, whereas PGR5-LIKE PHOTOSYNTHETIC PHENOTYPE1 (PGRL1) was highly enriched in the stroma thylakoids and practically missing from the grana cores. This article is part of a Special Issue entitled: Photosynthesis Research for Sustainability: Keys to Produce Clean Energy. (C) 2013 Elsevier B.V. All rights reserved.
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- Han, Guangye, et al.
(författare)
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Molecular basis for turnover inefficiencies (misses) during water oxidation in photosystem II
- 2022
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Ingår i: Chemical Science. - : Royal Society of Chemistry. - 2041-6520 .- 2041-6539. ; 13:29, s. 8667-8678
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Tidskriftsartikel (refereegranskat)abstract
- Photosynthesis stores solar light as chemical energy and efficiency of this process isv highly important. The electrons required for CO2 reduction are extracted from water in a reaction driven by light-induced charge separations in the Photosystem II reaction center and catalyzed by the CaMn4O5-cluster. This cyclic process involves five redox intermediates known as the S-0-S-4 states. In this study, we quantify the flash-induced turnover efficiency of each S state by electron paramagnetic resonance spectroscopy. Measurements were performed in photosystem II membrane preparations from spinach in the presence of an exogenous electron acceptor at selected temperatures between -10 degrees C and +20 degrees C and at flash frequencies of 1.25, 5 and 10 Hz. The results show that at optimal conditions the turnover efficiencies are limited by reactions occurring in the water oxidizing complex, allowing the extraction of their S state dependence and correlating low efficiencies to structural changes and chemical events during the reaction cycle. At temperatures 10 degrees C and below, the highest efficiency (i.e. lowest miss parameter) was found for the S-1 -> S-2 transition, while the S-2 -> S-3 transition was least efficient (highest miss parameter) over the whole temperature range. These electron paramagnetic resonance results were confirmed by measurements of flash-induced oxygen release patterns in thylakoid membranes and are explained on the basis of S state dependent structural changes at the CaMn4O5-cluster that were determined recently by femtosecond X-ray crystallography. Thereby, possible "molecular errors" connected to the e(-) transfer, H+ transfer, H2O binding and O-2 release are identified.
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- Mamedov, Fikret, et al.
(författare)
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Logistics in the life cycle of photosystem II during maturation : lateral movement in the thylakoid membrane and activation of the electron transfer
- 2003
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Ingår i: Physiologia Plantarum. - : Wiley-Blackwell. - 0031-9317 .- 1399-3054. ; 119:3, s. 328-336
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Forskningsöversikt (refereegranskat)abstract
- Due to its unique ability to split water, Photosystem II (PSII) is easily accessible to oxidative damage. Photoinhibited PSII centres diffuse laterally from the grana core region of the thylakoid membrane to the stroma lamellae in order to allow replacement of damaged proteins and cofactors. The ‘new born’ PSII centres in this region are characterized by the absence of the water splitting capacity and very poor ability to bind the secondary quinone acceptor, QB. After the repair process PSII has to regain the water splitting capacity. This requires a set of well-defined electron transfer reactions leading to assembly of the Mn-cluster. In order to minimize the danger of photoinhibition during these earlier stages of photoactivation of PSII, auxiliary donors to the primary donor P680+, such as redox active tyrosine on D2 protein, YD, and cytochrome b559 become involved in the electron transport reactions by providing necessary electrons. Cytochrome b559 may also serve as an electron acceptor to QA– if elevated light intensities occur during the photoactivation process. These reactions lead to activation of QB binding, and finally to the assembly of the Mn-cluster. All these electron transport events occur simultaneously with the lateral movement of PSII centres back to the appressed regions of the grana core, where the pool of the most active PSII is situated.
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