Recent advances in the structural biology of photosystem II

Photosystem II (PSII) is the membrane protein-pigment complex responsible for the light-driven oxidation of water to molecular oxygen, a reaction that enables the aerobic biosphere and powers biological carbon fixation. Over the past two decades, structural biology has transformed our understanding of PSII from low-resolution outlines of its protein chains and cofactors to near-atomic resolution models. Early X-ray crystallographic structures from thermophilic cyanobacteria established the architecture of the reaction centre and the Mn₄CaO₅ oxygen-evolving complex (OEC), defining the protein ligands and cofactor network that support charge separation and water oxidation. The advent of high-resolution single-particle cryo-EM microscopy has expanded structural coverage across taxa, assembly and repair intermediates, and PSII-antenna supercomplexes that are beyond crystallisation. CryoEM now routinely achieves sub-2.5 Å resolution. In situ cryo-EM tomography further bridges atomic models to the native thylakoid membrane environment, exposing the supramolecular organisation of PSII in cells. X-ray free electron laser (XFEL) pump-probe experiments provide time-resolved snapshots of the Kok S-state cycle, revealing substrate water insertion, metal-oxo rearrangements and approaches O-O bond formation. Despite these advances, key challenges remain, including unambiguous assignment of manganese oxidation states, direct localisation of hydrogen atoms and complete structural characterisation of transient S-state intermediates. Integration of structural methods with spectroscopy, computation and emerging protein design approaches promises not only deeper mechanistic insight into biological water oxidation, but also guidance for the development of robust, earth-abundant catalysts.