Peridinin-chlorophyll-protein complex the peridinin molecules to their neighboring chlorophyll molecule. PCP has served as a common model system for spectroscopy and for theoretical calculations relating to the protein's photophysics. PCP complexes are thought to occupy the thylakoid lumen. After energy transfer from the peridinin to the chlorophyll pigment, PCP complexes are believed to then transfer energy from the excited chlorophyll to membrane-bound light harvesting complexes. Peridinin-chlorophyll-protein complex The peridinin-chlorophyll-protein complex (PCP or PerCP) is a soluble molecular complex consisting of the peridinin-chlorophyll a-protein bound to peridinin, chlorophyll, and lipids. The peridinin molecules absorb light in the blue-green wavelengths (470 to 550 nm)
Photosystem I when they become photoexcited. Antenna molecules can absorb all wavelengths of light within the visible spectrum. The number of these pigment molecules varies from organism to organism. For instance, the cyanobacterium "Synechococcus elongatus" ("Thermosynechococcus elongatus") has about 100 chlorophylls and 20 carotenoids, whereas spinach chloroplasts have around 200 chlorophylls and 50 carotenoids. Located within the antenna complex of PSI are molecules of chlorophyll called P700 reaction centers. The energy passed around by antenna molecules is directed to the reaction center. There may be as many as 120 or as few as 25 chlorophyll molecules per P700. The P700 reaction center