Electron paramagnetic resonance and mutational analyses revealed the involvement of photosystem II-L subunit in the oxidation step of Tyr-Z by P680+ to form the Tyr-Z+P680Pheo- state in photosystem II.

@article{Hoshida1997ElectronPR,
  title={Electron paramagnetic resonance and mutational analyses revealed the involvement of photosystem II-L subunit in the oxidation step of Tyr-Z by P680+ to form the Tyr-Z+P680Pheo- state in photosystem II.},
  author={Hisashi Hoshida and Ryuji Sugiyama and Yoshiharu Nakano and Takashi Shiina and Yoshinori Toyoshima},
  journal={Biochemistry},
  year={1997},
  volume={36 40},
  pages={12053-61}
}
To reveal the molecular mechanism of involvement of photosystem II (PSII)-L protein in the electron transfer in PSII, effects of mutations in PSII-L on the photochemistry of PSII were investigated by means of electron paramagnetic resonance (EPR) and flash photolysis. Wild type and a series of mutant versions of PSII-L were overproduced in Escherichia coliand chromatographically purified. Plastoquinone 9 (PQ-9) depleted PSII reaction center core complex consisting of CP47/D1/D2/Cytb-559/PSII-I… CONTINUE READING