The intricate orchestration of electron transfer (ET) and proton transfer (PT) at the Mn4CaOn-cluster of photosystem II (PSII) is mechanistically pivotal but clearly insufficiently understood. Preparations of PSII membrane particles were investigated using a kinetically competent and sensitive method, photothermal beam deflection (PBD), to monitor apparent volume changes of the PSII protein. Driven by nanosecond laser flashes, the PSII was synchronously stepped through its water-oxidation cycle involving four (semi)stable states (S-0, S-1, S-2, and S-3) and minimally three additional transiently formed intermediates. The PBD approach was optimized as compared to our previous experiments, resulting in superior signal quality and resolution of more reaction steps. Now seven transitions were detected and attributed, according to the H/D-exchange, temperature, and pH effects on their time constants, to ET or PT events. The ET steps oxidizing the Mn4CaOn cluster in the S-2 -> S-3 and S-0 -> S-1 transitions, a biphasic PT prior to the O-2-evolving reaction, as well as the reoxidation of the primary quinone acceptor (QA-) at the PSII acceptor side were detected for the first time by PBD. The associated volume changes involve (i) initial formation of charged groups resulting in contraction assignable to electrostriction, (ii) volume contraction explainable by reduced metal-ligand distances upon manganese oxidation, and (iii) charge-compensating proton removal resulting in volume expansion due to electrostriction reversal. These results support a reaction cycle of water oxidation exhibiting alternate ET and PT steps. An extended kinetic scheme for the O-2-evolving S-3 double right arrow S-0 transition is proposed, which includes crucial structural and protonic events.