Functional and structural changes of the photosystem II complex induced by high irradiance in cyanobacterial cells
Language English Country Great Britain, England Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Photosynthetic Reaction Center Complex Proteins chemistry metabolism radiation effects MeSH
- Photosystem II Protein Complex MeSH
- Cyanobacteria radiation effects MeSH
- Light-Harvesting Protein Complexes * MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Photosynthetic Reaction Center Complex Proteins MeSH
- Photosystem II Protein Complex MeSH
- photosystem II, chlorophyll binding protein, CP-43 MeSH Browser
- photosystem II, chlorophyll-binding protein, CP-47 MeSH Browser
- Light-Harvesting Protein Complexes * MeSH
A gradual disintegration of the photosystem II (PSII) complex, initiated by a release of the chlorophyll-protein CP43, was identified during low-temperature illumination of Synechococcus cells. This process was slower compared to the decline of the PSII primary charge separation activity, and much slower than the photoinactivation of oxygen evolution. All three processes were slowed down in the presence of diuron. The results indicate that when the PSII repair was blocked, the inactivation of charge separation activity and the release of CP43 preceded the degradation of the D1 protein. In contrast, a much faster degradation of D1 connected to its rapid exchange was triggered by inactivation of oxygen evolution, and no disassembly of PSII was needed. We propose the existence of two different mechanisms of D1 degradation in the cells of the thermophilic cyanobacterium Synechococcus elongatus.
References provided by Crossref.org
The biogenesis and maintenance of PSII: Recent advances and current challenges
Making proteins green; biosynthesis of chlorophyll-binding proteins in cyanobacteria