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)
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