Peridinin-chlorophyll-protein complex 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) and transfer energy to the chlorophyll molecules with extremely high efficiency. PCP complexes are found in many photosynthetic dinoflagellates, in which they may be the primary light-harvesting complexes. The PCP protein has been identified in dinoflagellate genomes in at least two forms, a homodimeric form composed of two 15-kD monomers, and a monomeric form of around 32kD believed to have evolved from the
Thylakoid centers, each consisting of an antenna complex that uses chlorophylls and accessory photosynthetic pigments such as carotenoids and phycobiliproteins to harvest light at a variety of wavelengths. Each antenna complex has between 250 and 400 pigment molecules and the energy they absorb is shuttled by resonance energy transfer to a specialized chlorophyll "a" at the reaction center of each photosystem. When either of the two chlorophyll "a" molecules at the reaction center absorbs energy, an electron is excited and transferred to an electron-acceptor molecule. Photosystem I contains a pair of chlorophyll "a" molecules, designated P700, at its reaction center that