Release of the Oxygen-Evolving Complex Subunits from Photosystem II Membranes in Phosphorylation Condition under Light Stress
So far it is unclear whether the release of oxygen-evolving complex (OEC) subunits including PsbO, PsbP, and PsbQ proteins is affected by the phosphorylation of photosystem II (PSII) membranes under light stress. In this work, different phosphorylated PSII membranes were obtained from spinach. Phosp...
Saved in:
Published in | Chinese journal of chemistry Vol. 29; no. 12; pp. 2631 - 2636 |
---|---|
Main Author | |
Format | Journal Article |
Language | English |
Published |
Weinheim
WILEY-VCH Verlag
01.12.2011
WILEY‐VCH Verlag Wiley Subscription Services, Inc |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | So far it is unclear whether the release of oxygen-evolving complex (OEC) subunits including PsbO, PsbP, and PsbQ proteins is affected by the phosphorylation of photosystem II (PSII) membranes under light stress. In this work, different phosphorylated PSII membranes were obtained from spinach. Phosphorylation partially suppressed the release of PsbO, PsbP, and PsbQ proteins from PSII membranes under light stress. Reactive oxygen species including superoxide anion, hydrogen peroxide and hydroxyl radical, were involved in the release of a small part of PsbO protein, but not in the release of PsbP and PsbQ proteins in the non-phosphorylated and phosphorylated PSII membranes. All of the results suggested that the release of PsbO, PsbP, and PsbQ proteins was partially regulated by phosphorylation in PSII membranes, and the role of reactive oxygen species in the release of OEC subunits in non-phosphorylated PSII membranes was the same as in phosphorylated PSII membranes. |
---|---|
Bibliography: | 31-1547/O6 So far it is unclear whether the release of oxygen-evolving complex (OEC) subunits including PsbO, PsbP, and PsbQ proteins is affected by the phosphorylation of photosystem II (PSII) membranes under light stress. In this work, different phosphorylated PSII membranes were obtained from spinach. Phosphorylation partially suppressed the release of PsbO, PsbP, and PsbQ proteins from PSII membranes under light stress. Reactive oxygen species including superoxide anion, hydrogen peroxide and hydroxyl radical, were involved in the release of a small part of PsbO protein, but not in the release of PsbP and PsbQ proteins in the non-phosphorylated and phosphorylated PSII membranes. All of the results suggested that the release of PsbO, PsbP, and PsbQ proteins was partially regulated by phosphorylation in PSII membranes, and the role of reactive oxygen species in the release of OEC subunits in non-phosphorylated PSII membranes was the same as in phosphorylated PSII membranes. protein release, reactive oxygen species, EPR spectroscopy, radicals, photosystem II the Pilot Project of Knowledge Innovation Program of the Chinese Academy of Sciences - No. KJCX2-SW-w29 istex:619109CAF96B89FA25C993116F29D21E27551584 ark:/67375/WNG-4WMDM088-0 ArticleID:CJOC201180434 the National Natural Science Foundation of China - No. 20875093 and 90813021 |
ISSN: | 1001-604X 1614-7065 |
DOI: | 10.1002/cjoc.201180434 |