Abstract
This minireview summarizes the current state of knowledge concerning the role of Cl(-) in the oxygen-evolving complex (OEC) of photosystem II (PSII). The model that proposes that Cl(-) is a Mn ligand is discussed in light of more recent work. Studies of Cl(-) specificity, stoichiometry, kinetics, and retention by extrinsic polypeptides are discussed, as are the results that fail to detect Cl(-) ligation to Mn and results that show a lack of a requirement for Cl(-) in PSII-catalyzed H(2)O oxidation. Mutagenesis experiments in cyanobacteria and higher plants that produce evidence for a correlation between Cl(-) retention and stable interactions among intrinsic and extrinsic polypeptides are summarized, and spectroscopic data on the interaction between PSII and Cl(-) are discussed. Lastly, the question of the site of Cl(-) action in PSII is discussed in connection with the current crystal structures of the enzyme.
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