Water oxidation in Photosystem II is dependent on a particular amino acid residue, Tyrosine_Z. This is a redox intermediate in steady state oxygen evolution and transfers electrons from the water splitting CaMn₄ cluster to the central chlorophyll radical P₆₈₀⁺. This Perspective discusses the functional principles of Tyrosine_Z as a proton-coupled redox active link, as well as mechanistic studies of synthetic model systems and implications for artificial photosynthesis. Experimental studies of temperature dependence and kinetic isotope effects are important tools to understand these reactions. We emphasize the importance of proton transfer distance and hydrogen bond dynamics that are responsible for variation in the rate of PCET by several orders of magnitude. The mechanistic principles discussed and their functional significance are not limited to tyrosine and biological systems, but are important to take into account when constructing artificial photosynthetic systems. Of particular importance is the role of proton transfer management in water splitting and solar fuel catalysis.