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- W2277886966 abstract "Photosystem II (PSII), which catalyzes photosynthetic water oxidation, is composed of more than 20 subunits, including membrane-intrinsic and -extrinsic proteins. The PSII extrinsic proteins shield the catalytic Mn4CaO5 cluster from the outside bulk solution and enhance binding of inorganic cofactors, such as Ca2+ and Cl-, in the oxygen-evolving center (OEC) of PSII. Among PSII extrinsic proteins, PsbO is commonly found in all oxygenic organisms, while PsbP and PsbQ are specific to higher plants and green algae, and PsbU, PsbV, CyanoQ, and CyanoP exist in cyanobacteria. In addition, red algae and diatoms have unique PSII extrinsic proteins, such as PsbQ’ and Psb31, suggesting functional divergence during evolution. Recent studies with reconstitution experiments combined with Fourier transform infrared spectroscopy have revealed how the individual PSII extrinsic proteins affect the structure and function of the OEC in different organisms. In this review, we summarize our recent results and discuss changes that have occurred in the structural coupling of extrinsic proteins with the OEC during evolutionary history." @default.
- W2277886966 created "2016-06-24" @default.
- W2277886966 creator A5005651755 @default.
- W2277886966 creator A5040377353 @default.
- W2277886966 date "2016-02-05" @default.
- W2277886966 modified "2023-09-30" @default.
- W2277886966 title "Structural Coupling of Extrinsic Proteins with the Oxygen-Evolving Center in Photosystem II" @default.
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- W2277886966 doi "https://doi.org/10.3389/fpls.2016.00084" @default.
- W2277886966 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4743485" @default.
- W2277886966 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26904056" @default.
- W2277886966 hasPublicationYear "2016" @default.
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