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Tocopherol controls D1 amino acid oxidation by oxygen radicals in Photosystem II
A. Kumar, A. Prasad, M. Sedlářová, R. Kale, LK. Frankel, L. Sallans, TM. Bricker, P. Pospíšil
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, práce podpořená grantem, Research Support, U.S. Gov't, Non-P.H.S.
NLK
Free Medical Journals
od 1915 do Před 6 měsíci
Freely Accessible Science Journals
od 1915 do Před 6 měsíci
PubMed Central
od 1915 do Před 6 měsíci
Europe PubMed Central
od 1915 do Před 6 měsíci
Open Access Digital Library
od 1915-01-15
Open Access Digital Library
od 1915-01-01
PubMed
33479170
DOI
10.1073/pnas.2019246118
Knihovny.cz E-zdroje
- MeSH
- alfa-tokoferol chemie metabolismus MeSH
- aminokyseliny chemie metabolismus MeSH
- Arabidopsis enzymologie genetika účinky záření MeSH
- fotosyntéza fyziologie účinky záření MeSH
- fotosystém II - proteinový komplex chemie genetika metabolismus MeSH
- hydroxylový radikál chemie metabolismus MeSH
- interakční proteinové domény a motivy MeSH
- intramolekulární transferasy chemie genetika metabolismus MeSH
- konformace proteinů, alfa-helix MeSH
- konformace proteinů, beta-řetězec MeSH
- kyslík chemie metabolismus MeSH
- molekulární modely MeSH
- mutace MeSH
- oxidace-redukce MeSH
- superoxidy chemie metabolismus MeSH
- světlo MeSH
- termodynamika MeSH
- Thermosynechococcus enzymologie genetika účinky záření MeSH
- tylakoidy enzymologie genetika účinky záření MeSH
- vazba proteinů MeSH
- vazebná místa MeSH
- železo chemie metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Research Support, U.S. Gov't, Non-P.H.S. MeSH
Photosystem II (PSII) is an intrinsic membrane protein complex that functions as a light-driven water:plastoquinone oxidoreductase in oxygenic photosynthesis. Electron transport in PSII is associated with formation of reactive oxygen species (ROS) responsible for oxidative modifications of PSII proteins. In this study, oxidative modifications of the D1 and D2 proteins by the superoxide anion (O2•-) and the hydroxyl (HO•) radicals were studied in WT and a tocopherol cyclase (vte1) mutant, which is deficient in the lipid-soluble antioxidant α-tocopherol. In the absence of this antioxidant, high-resolution tandem mass spectrometry was used to identify oxidation of D1:130E to hydroxyglutamic acid by O2•- at the PheoD1 site. Additionally, D1:246Y was modified to either tyrosine hydroperoxide or dihydroxyphenylalanine by O2•- and HO•, respectively, in the vicinity of the nonheme iron. We propose that α-tocopherol is localized near PheoD1 and the nonheme iron, with its chromanol head exposed to the lipid-water interface. This helps to prevent oxidative modification of the amino acid's hydrogen that is bonded to PheoD1 and the nonheme iron (via bicarbonate), and thus protects electron transport in PSII from ROS damage.
Citace poskytuje Crossref.org
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- $a Kumar, Aditya $u Department of Biophysics, Centre of the Region Haná for Biotechnological and Agricultural Research, Faculty of Science, Palacký University, 771 47 Olomouc, Czech Republic
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