A model for the mechanism of chloride activation of oxygen evolution in photosystem II

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Abstract
A hypothesis is proposed to explain the function of Cl- in activating the oxygenevolving complex (OEC) of photosystem II (PS II), based on the results of recent 35Cl-NMR studies. The putative mechanism involves Cl- binding to two types of sites. An intrinsic site is suggested to be composed of three histidyl residues (His 332 and His 337 from D1 and His 337 D2). It is proposed that Cl- binding to this site accelerates the abstraction of H+ from water by raising the pKa's of the histidine imidazole groups. Cl- binding also stimulates the transfer of H+ from this intrinsic site to a set of extrinsic sites on the 33 kD extrinsic polypeptide. The extrinsic Cl- binding sites are suggested to involve four protein domains that are linked together by salt-bridge contacts. Chloride and H+ donated from the intrinsic site attack these intramolecular salt-bridges in a defined sequence, thereby exposing previously inaccessible Cl- and H+ binding sites and stimulating the oxidation of water. This hypothesis also proposes a possible structure for the Mn active site within the D1/D2 complex. Specific amino-acid residues that are likely to participate as Mn lignads are identified on the lumenal portions of the D1 and D2 proteins that are different from those in the L and M subunits of photosynthetic bacteria; the choice of these residues is based on the metal coordination chemistry of these residues, their location within the polypeptide chain, the regularity of their spacing, and their conservation through evolution. The catalytic Mn-binding residues are suggested to be D-61, E-65, E-92, E-98, D-103; D-308, E-329, E-342 and E-333 in D1, and H-62, E-70, H-88, E-97, D-101; E-313, D-334, E-338 and E-345 in D2. Finally, this hypothesis identifies sites on both D2 and the 33 kD extrinsic polypeptide that might be involved in high- and low-affinity Ca2+ binding.

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