perfine structure indicative of an exchange-coupled manganese center in signals near g = 4 in ammonia-treated PS II preparations.In addition, Baumgarten et al.34 measured light-induced changes in the magnetic susceptibility of fluoride-treated PS II preparations, which exhibit an altered EPR signal at g -4.2 in the S2 state,7•35 that they interpreted as evidence of a magnetically coupled site. These chemically inhibited preparations, although giving rise to altered EPR properties, have been considered as possible analogues for the native g = 4.1 species, with the suggestion that both this signal and the multiline signal may originate from the same multinuclear cluster. However, we note that addition of exogenous ligands has been seen to significantly alter exchange couplings and bridging structure within multisite metalloprotein complexes, either by disrupting existing bridges or by leading to

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