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 completed by Ian Fleming, and in 1990 Woodward and co-authors published an updated synthesis. Chlorophyll f was announced to be present in cyanobacteria and other oxygenic microorganisms that form stromatolites in 2010; a molecular formula of CHONMg and a structure of (2-formyl)-chlorophyll "a" were deduced based on NMR, optical and mass spectra. Chlorophyll is vital for photosynthesis, which allows plants to absorb energy from light. Chlorophyll molecules are arranged in and around photosystems that are embedded in the thylakoid membranes of chloroplasts. In these complexes, chlorophyll serves three functions. The function of the vast majority of chlorophyll (up to several