Comparisons of enzyme efficiency and electron transfer show that, to oxidize water using lower energy light, the two types of far-red photosystem II have adopted opposite trade-offs between efficiency of light use and resilience to light damage.

The nature of the phycobilisome–photosystem II supercomplex on the native thylakoid determined with cryo-electron tomography at an unprecedented resolution reveals that one phycobilisome interconnects with six photosystem monomers.

The structures of photosystem II, with the water-oxidizing Mn4CaO5-cluster fully removed and in an intermediate assembly state, show that photoassembly is facilitated by perfectly pre-arranged protein ligands of the five metal ions.

Oxidative modification of Tryptophan residues in the reaction center protein D1 may be a key to drive the Photosystem II repair, likely enhancing accessibility of FtsH protease to D1.

Storage of solar energy in the thylakoid electrical field by photosynthesis in vivo can substantially destabilize charge-separated states in photosystem II, leading to singlet oxygen production and photodamage, contributing to loss of productivity, especially under fluctuating light experienced in the field.

Photosystem II, the pigment-protein complex responsible for water oxidation in photosynthesis, was found to exist in two different core conformations with altered antennae connectivity.

The structure of the photosystem I (PSI) complex from Synechocystis is determined, and reaction center subunits engineered to resemble a viral PSI are found to promote promiscuous electron acceptor properties.

Two species of photosynthetic cyanobacteria can thrive in far-red light but they either become less resilient to photodamage or less energy efficient.

Slug chloroplasts avoid damage to photosynthesis by maintaining an oxidized electron transfer chain with the help of oxygen-sensitive electron acceptors.

Coupled physiology and gene expression, measured over a two-day time course, reveals specific time-of-day responses to the early stages of drought in Brassica rapa.