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.

The cells of a cyanobacterium act as spherical micro-lenses, allowing the cell to see a light source and move towards it.

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.

Colour-controlled c-di-GMP signalling mediates directional switch of phototaxis via within-a-pole regulation of type IV pili in rod-shaped cyanobacteria Thermosynechococcus vulcanus.

Primordial cyanobacterial PSI structure.

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 necessity of studying extremophile organisms is exemplified by the structure of photosystem I from a high-light tolerant cyanobacteria, demonstrating the relationship between the structure and function in photosystem I.

Synechocystis switches its redox pools under reducing photomixotrophic conditions from utilizing NAD(H)- to ferredoxin-dependent enzymes and thereby balances its metabolism in a trade-off between energy conservation and chemical driving forces.