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
Chlorophyll directly absorbing light and performing charge separation events without the assistance of other chlorophyll pigments, but the probability of that happening under a given light intensity is small. Thus, the other chlorophylls in the photosystem and antenna pigment proteins all cooperatively absorb and funnel light energy to the reaction center. Besides chlorophyll "a", there are other pigments, called accessory pigments, which occur in these pigment–protein antenna complexes. Chlorophylls are numerous in types, but all are defined by the presence of a fifth ring beyond the four pyrrole-like rings. Most chlorophylls are classified as chlorins, which are reduced relatives to porphyrins