| Autor: |
Shan J; Key Laboratory of Biomacromolecules (CAS), National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.; College of Life Sciences, University of Chinese Academy of Sciences, Beijing 100049, China., Niedzwiedzki DM; Center for Solar Energy and Energy Storage, Washington University in St. Louis, St. Louis, MO 63130, USA.; Department of Energy, Environmental, & Chemical Engineering, Washington University in St. Louis, St. Louis, MO 63130, USA., Tomar RS; Department of Biology, Saint Louis University, St. Louis, MO, 63103, USA., Liu Z; Key Laboratory of Biomacromolecules (CAS), National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.; College of Life Sciences, University of Chinese Academy of Sciences, Beijing 100049, China., Liu H; Department of Biology, Saint Louis University, St. Louis, MO, 63103, USA. |
| Abstrakt: |
Photosystem II (PSII) splits water in oxygenic photosynthesis on Earth. The structure and function of the C 4 S 4 M 2 -type PSII-LHCII (light-harvesting complex II) megacomplexes from the wild-type and PsbR-deletion mutant plants are studied through electron microscopy (EM), structural mass spectrometry, and ultrafast fluorescence spectroscopy [time-resolved fluorescence (TRF)]. The cryo-EM structure of a type I C 4 S 4 M 2 megacomplex demonstrates that the three domains of PsbR bind to the stromal side of D1, D2, and CP43; associate with the single transmembrane helix of the redox active Cyt b 559 ; and stabilize the luminal extrinsic PsbP, respectively. This megacomplex, with PsbR and PsbY centered around the narrow interface between two dimeric PSII cores, provides the supramolecular structural basis that regulates the plastoquinone occupancy in Q B site, excitation energy transfer, and oxygen evolution. PSII-LHCII megacomplexes (types I and II) and LHC aggregation levels in Arabidopsis psbR mutant were also interrogated and compared to wild-type plants through EM and picosecond TRF. |
