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The molecular oxygen we breathe is produced from water-derived oxygen species bound to the Mn 4 CaO 5 cluster in photosystem II (PSII). Present research points to the central oxo-bridge O5 as the 'slow exchanging substrate water (W s )', while, in the S 2 state, the terminal water ligands W2 and W3 are both discussed as the 'fast exchanging substrate water (W f )'. A critical point for the assignment of W f is whether or not its exchange with bulk water is limited by barriers in the channels leading to the Mn 4 CaO 5 cluster. In this study, we measured the rates of H 2  16 O/H 2  18 O substrate water exchange in the S 2 and S 3 states of PSII core complexes from wild-type (WT) Synechocystis sp. PCC 6803, and from two mutants, D1-D61A and D1-E189Q, that are expected to alter water access via the Cl1/O4 channels and the O1 channel, respectively. We found that the exchange rates of W f and W s were unaffected by the E189Q mutation (O1 channel), but strongly perturbed by the D61A mutation (Cl1/O4 channel). It is concluded that all channels have restrictions limiting the isotopic equilibration of the inner water pool near the Mn 4 CaO 5 cluster, and that D61 participates in one such barrier. In the D61A mutant this barrier is lowered so that W f exchange occurs more rapidly. This finding removes the main argument against Ca-bound W3 as fast substrate water in the S 2 state, namely the indifference of the rate of W f exchange towards Ca/Sr substitution.

chemical science

The exchange of the fast substrate water in the S<sub>2</sub> state of photosystem II is limited by diffusion of bulk water through channels – implications for the water oxidation mechanism

The exchange of the fast substrate water in the S2 state of photosystem II is limited by diffusion of bulk water through channels – implications for the water oxidation mechanism

The exchange of the fast substrate water in the S₂ state of photosystem II is limited by diffusion of bulk water through channels – implications for the water oxidation mechanism