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
Photosynthesis Cycle. Nobel Prize-winning scientist Rudolph A. Marcus was able to discover the function and significance of the electron transport chain. Otto Heinrich Warburg and Dean Burk discovered the I-quantum photosynthesis reaction that splits the CO, activated by the respiration. In 1950, first experimental evidence for the existence of photophosphorylation "in vivo" was presented by Otto Kandler using intact "Chlorella" cells and interpreting his findings as light-dependent ATP formation. In 1954, Daniel I. Arnon et al. discovered photophosphorylation "in vitro" in isolated chloroplasts with the help of P. Louis N.M. Duysens and Jan Amesz discovered that chlorophyll a will absorb one