The oxygen-evolving complex (OEC) of photosystem II (PSII) is a unique Mn4O5Ca cluster that catalyzes water oxidation via four photoactivated electron transfer steps. As the protein influence on the redox and protonation chemistry of the OEC remains an open question, we present a classical valence model of the OEC that allows the redox state of each Mn and the protonation state of bridging mu-oxos and terminal waters to remain in equilibrium with the PSII protein throughout the redox cycle. We find that the last bridging oxygen loses its proton during the transition from S-0 to S-1. Two possible S-2 states are found depending on the OEC geometry: S-2 has Mn4(IV) with a proton lost from a terminal water (W1) trapped by the nearby D1-D61 if O5 is closer to Mn4, or Mn1 (IV), with partial deprotonation of D1-H337 and D1-E329 if O5 is closer to Mill. In S-3, the OEC is Mn-4(IV) with W2 deprotonated. The estimated OEC E-m's range from +0.7 to +1.3 V, enabling oxidation by P-680(+), the primary electron donor in PSII. In chloride-depleted PSII, the proton release increases during the S-1, to S-2 transition, leaving the OEC unable to properly advance through the water-splitting cycle.