The recently-published 3.5 Å resolution X-ray crystal structure of a cyanobacterial photosystem II (PDB entry 1S5L) provides a detailed architecture of the oxygen-evolving complex (OEC) and the surrounding amino-acids [K. N. Ferreira, T. M. Iverson, K. Maghlaoui, J. Barber and S. Iwata, Science, 2004, 203, 1831-1838. The revealed geometry of the OEC lends weight to certain hypothesized mechanisms for water-splitting, including the one propounded by this group, in which a calcium-bound water acts as a nucleophile to attack the oxygen of a Mn V QO group in the crucial O-O bond-forming step [J. S. Vrettos, J. Limburg and G. W. Brudvig, Biochim. Biophys. Acta, 2001Acta, , 1503. Here we re-examine this mechanism in the light of the new crystallographic information and make detailed suggestions concerning the mechanistic functions (especially the redox and protontransfer roles) of calcium, chloride and certain amino-acid residues in and around the OEC. In particular, we propose an important role for an arginine residue, CP43-Arg357, in abstracting protons from a substrate water molecule during the water-splitting reaction.