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A light-harvesting complex consists of a number of chromophores [1] which are complex subunit proteins that may be part of a larger super complex of a photosystem, the functional unit in photosynthesis. It is used by plants and photosynthetic bacteria to collect more of the incoming light than would be captured by the photosynthetic reaction ...
A variety in light-harvesting complexes exist across the photosynthetic species. Green plants and algae have two different types of reaction centers that are part of larger supercomplexes known as P700 in Photosystem I and P680 in Photosystem II. The structures of these supercomplexes are large, involving multiple light-harvesting complexes.
The light harvesting complex (LHC) inside the chloroplasts of Lichen is activated when subjected to darkness. [ 8 ] Gasulla, Casano and Guéra, noticed that this increase in LHC activity caused PS II and the PQ pool within lichen to decrease, indicating the initiation of chlororespiration.
The light-harvesting complex (or antenna complex; LH or LHC) is an array of protein and chlorophyll molecules embedded in the thylakoid membrane of plants and cyanobacteria, which transfer light energy to one chlorophyll a molecule at the reaction center of a photosystem. The antenna pigments are predominantly chlorophyll b, xanthophylls, and ...
Reaction centers are multi-protein complexes found within the thylakoid membrane. At the heart of a photosystem lies the reaction center, which is an enzyme that uses light to reduce and oxidize molecules (give off and take up electrons). This reaction center is surrounded by light-harvesting complexes that enhance the absorption of light.
The light-harvesting system of PSI uses multiple copies of the same transmembrane proteins used by PSII. The energy of absorbed light (in the form of delocalized, high-energy electrons) is funneled into the reaction center, where it excites special chlorophyll molecules (P700, with maximum light absorption at 700 nm) to a higher energy level.
The light harvesting complex in purple bacteria is multifunctional; at high light intensities, the light harvesting complex typically switches into a quenched state through a conformational change of the PPC, and at low light intensities, the light harvesting complex typically reverts to an unquenched state. [11] These conformational changes ...
The phycobiliproteins themselves show little sequence evolution due to their highly constrained function (absorption and transfer of specific wavelengths). [ citation needed ] In some species of cyanobacteria, when both phycocyanin and phycoerythrin is present, the phycobilisome can undergo significant restructuring as response to light color.