Peridinin-chlorophyll-protein complex by the CATH database, which systematically classifies protein structures, as an "alpha solenoid" fold; however, elsewhere in the literature the term alpha solenoid is used for open and less compact helical protein structures. Photosynthetic dinoflagellates contain membrane-bound light-harvesting complexes similar to those found in green plants. They additionally contain water-soluble protein-pigment complexes that exploit carotenoids such as peridinin to extend their photosynthetic capacity. Peridinin absorbs light in the blue-green wavelengths (470 to 550 nm) which are inaccessible to chlorophyll by itself; instead the PCP complex uses the geometry of the relative pigment orientations to effect extremely high-efficiency energy transfer from
Photodissociation chlorophyll molecule (P680, where P stands for pigment and 680 for its absorption maximum at 680 nm) in the reaction center of photosystem II via resonance energy transfer. P680 can also directly absorb a photon at a suitable wavelength. Photolysis during photosynthesis occurs in a series of light-driven oxidation events. The energized electron (exciton) of P680 is captured by a primary electron acceptor of the photosynthetic electron transfer chain and thus exits photosystem II. In order to repeat the reaction, the electron in the reaction center needs to be replenished. This occurs by oxidation of water in the case of