Oxidative modifications of the Photosystem II D1 protein by reactive oxygen species: from isolated protein to cyanobacterial cells
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- fotosystém II - proteinový komplex analýza chemie MeSH
- hem chemie metabolismus MeSH
- ligandy MeSH
- molekulární sekvence - údaje MeSH
- mutace MeSH
- oxidace-redukce MeSH
- peptidové fragmenty chemie metabolismus MeSH
- peroxid vodíku farmakologie MeSH
- reaktivní formy kyslíku antagonisté a inhibitory farmakologie MeSH
- sbalování proteinů MeSH
- sekvence aminokyselin MeSH
- sinice chemie účinky léků genetika MeSH
- superoxidy farmakologie MeSH
- světlo MeSH
- tylakoidy chemie účinky léků účinky záření MeSH
- železo chemie metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- fotosystém II - proteinový komplex MeSH
- hem MeSH
- ligandy MeSH
- peptidové fragmenty MeSH
- peroxid vodíku MeSH
- reaktivní formy kyslíku MeSH
- superoxidy MeSH
- železo MeSH
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 D1-specific cleavage. The D1 modification, fragmentation and cross-linking were suppressed by ROS scavengers, supporting the direct role of ROS in these phenomena. Identical symptoms of the ROS-induced D1 damage were detected in illuminated cells of Synechocystis mutants with a higher probability of ROS formation, documenting the relevance of the in vitro results for the situation in vivo.
Citace poskytuje Crossref.org
Tocopherol controls D1 amino acid oxidation by oxygen radicals in Photosystem II
Characterization of Protein Radicals in Arabidopsis
