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
Anoxygenic photosynthesis Anoxygenic photosynthesis The pigments used to carry out anaerobic photosynthesis are similar to chlorophyll but differ in molecular detail and peak wavelength of light absorbed. Bacteriochlorophylls "a" through "g" absorb electromagnetic photons maximally in the near-infrared within their natural membrane milieu. This differs from chlorophyll a, the predominant plant and cyanobacteria pigment, which has peak absorption wavelength approximately 100 nanometers shorter (in the red portion of the visible spectrum). Some archaea (e.g. "Halobacterium") capture light energy for metabolic function and are thus phototrophic but none are known to "fix" carbon (i.e. be photosynthetic). Instead of a chlorophyll-type receptor and electron