title: Photosynthetic water oxidation: The protein framework.
abstract: Approximately 20 protein subunits are associated with the PS II complex, not counting subunits of peripheral light-harvesting antenna complexes. However, it is not yet established which proteins specifically are involved in the water-oxidation process. Much evidence supports the concept that the D1/D2 reaction center heterodimer not only plays a central role in the primary photochemistry of Photosystem II, but also is involved in electron donation to P680 and in ligation of the manganese cluster. This evidence includes (a) the primary donor to P680 has been shown to be a redox-active tyrosyl residue (Tyr161) in the D1 protein, and (b) site-directed mutagenesis and computer-assisted modeling of the reaction center heterodimer have suggested several sites with a possible function in manganese ligation. These include Asp170, Gln165 and Gln189 of the D1 protein and Glu69 of the D2 protein as well as the C-terminal portion of the mature D1 protein. Also, hydrophilic loops of the chlorophyll-binding protein CP43 that are exposed at the inner thylakoid surface could be essential for the water-splitting process.In photosynthetic eukaryotes, three lumenal extrinsic proteins, PS II-O (33 kDa), PS II-P (23 kDa) and PS II-Q (16 kDa), influence the properties of the manganese cluster without being involved in the actual catalysis of water oxidation. The extrinsic proteins together may have multiple binding sites to the integral portion of PS II, which could be provided by the D1/D2 heterodimer and CP47. A major role for the PS II-O protein is to stabilize the manganese cluster. Most experimental evidence favors a connection of the PS II-P protein with binding of the Cl(-) and Ca(2+) ions required for the water oxidation, while the PS II-Q protein seems to be associated only with the Cl(-) requirement. The two latter proteins are not present in PS II of prokaryotic organisms, where their functions may be replaced by a 10-12 kDa subunit and a newly discovered low-potential cytochrome c-550.
authors: Department of Biochemistry, Arrhenius Laboratories for Natural Sciences, Stockholm University, S-106 91, Stockholm, Sweden.
authors: W F
authors: WF
authors: Vermaas
authors: S
authors: S
authors: Styring
authors: W P
authors: WP
authors: Schröder
authors: B
authors: B
authors: Andersson