Open AccessHigh-resolution cryo-electron microscopy structure of photosystem II from the mesophilic cyanobacterium, Synechocystis sp. PCC 6803
Author(s) -
Christopher J. Gisriel,
Jimin Wang,
Jinchan Liu,
David A. Flesher,
Krystle Reiss,
Hao-Li Huang,
Ke Yang,
William H. Armstrong,
M. R. Gunner,
Víctor S. Batista,
Richard J. Debus,
Gary W. Brudvig
Publication year - 2021
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2116765118
Subject(s) - photosystem ii , cyanobacteria , synechocystis , photosynthesis , oxidoreductase , photosystem i , chemistry , biophysics , thermophile , photochemistry , biology , biochemistry , bacteria , enzyme , genetics
Significance Photosystem II (PSII) is a photo-oxidoreductase that harnesses light energy to use water to make fuel. Water oxidation occurs at a metal cluster in the active site called the oxygen-evolving complex (OEC). Understanding PSII function has provided design principles for synthetic solar fuel catalysts; however, the details of water oxidation are obscured by the multiple states through which the mechanism proceeds, differences between species, and lability of the OEC. To better understand PSII function, we solved its structure fromSynechocystis sp. PCC 6803. We observe significant differences compared with PSII from thermophilic cyanobacteria that highlight the need for reexamination of previous data using this structure for interpretation. The structure also provides a platform for studies of site-directed mutations of PSII.