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N. Knoepfle, T. Bricker, C. Putnam-Evans (1999)
Site-directed mutagenesis of basic arginine residues 305 and 342 in the CP 43 protein of photosystem II affects oxygen-evolving activity in Synechocystis 6803.Biochemistry, 38 5
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Site-directed mutagenesis of the basic residues 321K to321 G in the CP 47 protein of photosystem II alters the chloride requirement for growth and oxygen-evolving activity in Synechocystis 6803Plant Molecular Biology, 34
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L. Frankel, T. Bricker (1989)
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The crystallographic data available for Photosystem II (PS II) in cyanobacteria has now provided complete structures for loop E from CP43 and CP47 as well as the extrinsic subunits PsbO, PsbU and PsbV. Protein interactions between these subunits are essential for stable water splitting and there is evidence that the binding of PsbU facilitates optimal energy transfer from the phycobilisome. Interactions between PsbO and CP47 may also play a role in dimer stabilization while loop E of CP43 contributes directly to the water-splitting reaction. Recent evidence also suggests that homologs of PsbP and PsbQ play key roles in cyanobacterial PS II, and under nutrient-deficient conditions PsbQ appears essential for photoautotrophic growth.
Photosynthesis Research – Springer Journals
Published: Jan 18, 2005
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