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 completed by Ian Fleming, and in 1990 Woodward and co-authors published an updated synthesis. Chlorophyll f was announced to be present in cyanobacteria and other oxygenic microorganisms that form stromatolites in 2010; a molecular formula of CHONMg and a structure of (2-formyl)-chlorophyll "a" were deduced based on NMR, optical and mass spectra. Chlorophyll is vital for photosynthesis, which allows plants to absorb energy from light. Chlorophyll molecules are arranged in and around photosystems that are embedded in the thylakoid membranes of chloroplasts. In these complexes, chlorophyll serves three functions. The function of the vast majority of chlorophyll (up to several