Here we use crystal structures to investigate and review channels and pathways for the transfer of substrates (water, plastoquinone (PQ)) and products (electrons, protons, oxygen, reduced PQ (PQH(2))) to, and from, the redox active catalytic sites of photosystem II (PSII). A putative oxygen channel has been identified which is about 21A in length, leading from the water splitting site to the lumen. This channel follows a path along the lumenal surface of CP43, passing across the interface of the large extrinsic loop which joins the fifth and sixth transmembrane helices of this chlorophyll binding protein. In so doing it seems to minimise interactions with the excited states of chlorophylls bound within the PSII complex, especially those that constitute the primary electron donor, P680. Two additional channels leading from the water splitting site, and also exiting at the lumen, were also identified. Their hydrophilic nature suggests that they probably facilitate the delivery of water to, and protons from, the catalytic site. Also discussed are unique features in the electron transfer pathway of PSII, as compared with those of purple photosynthetic bacteria, and structural implications of the PSII Q(B)-site in terms of PQ protonation and PQ/PQH(2) diffusion.