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)
Light-harvesting complexes of green plants protons and electrons. Under changing light conditions, the reversible phosphorylation of light harvesting chlorophyll a/b binding proteins (LHCII) represents a system for balancing the excitation energy between the two photosystems. The N-terminus of the chlorophyll A-B binding protein extends into the stroma where it is involved with adhesion of granal membranes and photo-regulated by reversible phosphorylation of its threonine residues. Both these processes are believed to mediate the distribution of excitation energy between photosystems I and II. This family also includes the photosystem II protein PsbS, which plays a role in energy-dependent quenching that increases thermal dissipation of excess absorbed