About: Oxidative modifications of the Photosystem II D1 protein by reactive oxygen species: From isolated protein to cyanobacterial cells     Goto   Sponge   NotDistinct   Permalink

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  • Action of reactive oxygen species (ROS) on the isolated D1 protein, a key component of Photosystem II (PSII) complex, was studied and compared with the effect of high irradiance on this protein in mildly solubilized photosynthetic membranes and cells of the cyanobacterium. Synechocystis. Whereas singlet oxygen caused mainly protein modification reflected by shift of its electrophoretic mobility, action of hydrogen peroxide and superoxide resulted in generation of specific fragments. Hydroxyl radicals as the most ROS induced fast disappearance of the protein. The results substantiate the ability of ROS to cause direct scission of the D1 peptide bonds. Similar D1 modification, fragmentation and additionally cross-linking with other PSII subunits were observed during illumination or hydrogen peroxide treatment of mildly solubilized thylakoids. Peroxide-induced fragmentation did not occur in thylakoids of the strain lacking a ligand to the nonheme iron, confirming the role of this prosthetic group in the
  • Action of reactive oxygen species (ROS) on the isolated D1 protein, a key component of Photosystem II (PSII) complex, was studied and compared with the effect of high irradiance on this protein in mildly solubilized photosynthetic membranes and cells of the cyanobacterium. Synechocystis. Whereas singlet oxygen caused mainly protein modification reflected by shift of its electrophoretic mobility, action of hydrogen peroxide and superoxide resulted in generation of specific fragments. Hydroxyl radicals as the most ROS induced fast disappearance of the protein. The results substantiate the ability of ROS to cause direct scission of the D1 peptide bonds. Similar D1 modification, fragmentation and additionally cross-linking with other PSII subunits were observed during illumination or hydrogen peroxide treatment of mildly solubilized thylakoids. Peroxide-induced fragmentation did not occur in thylakoids of the strain lacking a ligand to the nonheme iron, confirming the role of this prosthetic group in the (en)
  • Působení reaktivních forem kyslíku (ROS) na izolovaný protein D1, klíčovou podjednotku fotosystému II (PSII), bylo srovnáváno s působením vysoké ozářenosti na tento protein v solubilizovaných membránách a buňkách sinice Synechocystis sp. PCC 6803. Zatímco singletní kyslík způsoboval oxidaci proteinu spojenou se snížením mobility proteinu během elektroforézy, účinek peroxidu vodíku a superoxidu měl za následek tvorbu specifických fragmentů. Hydroxylové radikály způsobovaly rychlé mizení proteinu. Výsledky ukázaly schopnost ROS přímo štěpit peptidické vazby proteinu D1. Podobné modifikace, fragmentace a navíc zesítění s jinými proteiny vykazoval i protein D1 v ozářených membránách sinice. K tvorbě specifických fragmentů nedocházelo v membránách kmene bez nehemově vázaného železa na akceptorové straně PSII, ukazující zásadní roli této skupiny ve fragmentaci D1. Podobné symptomy oxidace ROS vykazoval i D1 protein v buňkách některých mutant, což potvrdilo relevanci výsledků získaných in vitro pro situaci (cs)
Title
  • Oxidativní modifikace bílkoviny D1 fotosystému II reaktivními formami kyslíku: od izolovaného proteinu k buňkám sinice (cs)
  • Oxidative modifications of the Photosystem II D1 protein by reactive oxygen species: From isolated protein to cyanobacterial cells
  • Oxidative modifications of the Photosystem II D1 protein by reactive oxygen species: From isolated protein to cyanobacterial cells (en)
skos:prefLabel
  • Oxidativní modifikace bílkoviny D1 fotosystému II reaktivními formami kyslíku: od izolovaného proteinu k buňkám sinice (cs)
  • Oxidative modifications of the Photosystem II D1 protein by reactive oxygen species: From isolated protein to cyanobacterial cells
  • Oxidative modifications of the Photosystem II D1 protein by reactive oxygen species: From isolated protein to cyanobacterial cells (en)
skos:notation
  • RIV/60076658:12640/04:00005425!RIV/2005/MSM/126405/N
http://linked.open.../vavai/riv/strany
  • 152-162
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(GA203/00/1257), P(LN00A141), Z(AV0Z5020903)
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  • 2
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
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http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
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  • 578684
http://linked.open...ai/riv/idVysledku
  • RIV/60076658:12640/04:00005425
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • amino-acid-residues;acceptor-side;Synechocystis PCC-6803;in-vivo;singlet oxygen;cross-linking;donor side;degradation;photoinhibition;light (en)
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http://linked.open...odStatuVydavatele
  • US - Spojené státy americké
http://linked.open...ontrolniKodProRIV
  • [5159A45670F3]
http://linked.open...i/riv/nazevZdroje
  • Photochemistry and Photobiology
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 79
http://linked.open...iv/tvurceVysledku
  • Komenda, Josef
  • Lupínková, Lenka
http://linked.open...n/vavai/riv/zamer
issn
  • 0031-8655
number of pages
http://localhost/t...ganizacniJednotka
  • 12640
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