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 c around 447, 580, 627 nm and 450, 581, 629 nm in diethyl ether and acetone respectively. Chlorophyll c is a form of chlorophyll "c" found in microalga "Emiliania huxleyi", identified in 1989. Its absorption maxima are around 452, 585, 625 nm and 452, 585, 627 nm in diethyl ether and acetone respectively. Chlorophyll c Chlorophyll "c" is a form of chlorophyll found in certain marine algae, including the photosynthetic Chromista (e.g. diatoms, brown algae) and dinoflagellates. It has a blue-greenish color and is an accessory pigment, particularly significant in its absorption of light in the 447-452 nm wavelength region, Like