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Significance Metal clusters play important roles in a wide variety of proteins. In cyanobacteria, algae, and plants, photosystem II uses light energy to oxidize water and release O2 at an active site that contains 1 calcium and 4 manganese atoms. This cluster must be built within the protein environment through a process known as photoassembly. Through experiments and simulations, we found that the efficiency of photoassembly was highly dependent on protons and chloride. Surprisingly, when the solvent was switched from H2 O to deuterated water, D2 O, the yield of photoassembly was higher. These results provide insights into the stepwise mechanism of photoassembly that can inform synthesis and repair strategies being developed for artificial photosynthesis technologies.

Photosystem II oxygen-evolving complex photoassembly displays an inverse H/D solvent isotope effect under chloride-limiting conditions