Phycobilisome
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Phycobilisome
Phycobilisomes are light harvesting antennae of photosystem II in cyanobacteria, red algae and glaucophytes. It was lost in the plastids of green algae / plants (chloroplasts). General structure Phycobilisomes are protein complexes (up to 600 polypeptides) anchored to thylakoid membranes. They are made of stacks of chromophorylated proteins, the phycobiliproteins, and their associated linker polypeptides. Each phycobilisome consists of a core made of allophycocyanin, from which several outwardly oriented rods made of stacked disks of phycocyanin and (if present) phycoerythrin(s) or phycoerythrocyanin. The spectral property of phycobiliproteins are mainly dictated by their prosthetic groups, which are linear tetrapyrroles known as phycobilins including phycocyanobilin, phycoerythrobilin, phycourobilin and phycobiliviolin. The spectral properties of a given phycobilin is influenced by its protein environment. Function Each phycobiliprotein has a specific absorption and f ...
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Light Harvesting Complex
A light-harvesting complex consists of a number of chromophores 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 center alone. The light which is captured by the chromophores is capable of exciting molecules from their ground state to a higher energy state, known as the excited state. This excited state does not last very long and is known to be short-lived. Light-harvesting complexes are found in a wide variety among the different photosynthetic species, with no homology among the major groups. The complexes consist of proteins and photosynthetic pigments and surround a photosynthetic reaction center to focus energy, attained from photons absorbed by the pigment, toward the reaction center using Förster resonance energy transfer. Function Photosynthesis ...
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Phycoerythrin
Phycoerythrin (PE) is a red protein-pigment complex from the light-harvesting phycobiliprotein family, present in cyanobacteria, red algae and cryptophytes, accessory to the main chlorophyll pigments responsible for photosynthesis.The red pigment is due to the prosthetic group, phycoerythrobilin, which gives phycoerythrin its red color. Like all phycobiliproteins, it is composed of a protein part covalently binding chromophores called phycobilins. In the phycoerythrin family, the most known phycobilins are: phycoerythrobilin, the typical phycoerythrin acceptor chromophore. Phycoerythrobilin is a linear tetrapyrrole molecule found in cyanobacteria, red algae, and cryptomonads. Together with other bilins such as phycocyanobilin it serves as a light-harvesting pigment in the photosynthetic light-harvesting structures of cyanobacteria called phycobilisomes. Phycoerythrins are composed of (αβ) monomers, usually organised in a disk-shaped trimer (αβ)3 or hexamer (αβ)6 (second ...
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Phycocyanin
Phycocyanin is a pigment-protein complex from the light-harvesting phycobiliprotein family, along with allophycocyanin and phycoerythrin. It is an accessory pigment to chlorophyll. All phycobiliproteins are water-soluble, so they cannot exist within the membrane like carotenoids can. Instead, phycobiliproteins aggregate to form clusters that adhere to the membrane called phycobilisomes. Phycocyanin is a characteristic light blue color, absorbing orange and red light, particularly near 620 nm (depending on which specific type it is), and emits fluorescence at about 650 nm (also depending on which type it is). Allophycocyanin absorbs and emits at longer wavelengths than phycocyanin C or phycocyanin R. Phycocyanins are found in cyanobacteria (also called blue-green algae). Phycobiliproteins have fluorescent properties that are used in immunoassay kits. Phycocyanin is from the Greek '' phyco'' meaning “algae” and ''cyanin'' is from the English word “cyan", which conven ...
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Phycobiliprotein
Phycobiliproteins are water-soluble proteins present in cyanobacteria and certain algae (rhodophytes, cryptomonads, glaucocystophytes). They capture light energy, which is then passed on to chlorophylls during photosynthesis. Phycobiliproteins are formed of a complex between proteins and covalently bound phycobilins that act as chromophores (the light-capturing part). They are most important constituents of the phycobilisomes. Major phycobiliproteins Characteristics Phycobiliproteins demonstrate superior fluorescent properties compared to small organic fluorophores, especially when high sensitivity or multicolor detection required : * Broad and high absorption of light suits many light sources * Very intense emission of light: 10-20 times brighter than small organic fluorophores * Relative large Stokes shift gives low background, and allows multicolor detections. * Excitation and emission spectra do not overlap compared to conventional organic dyes. * Can be used in tandem ...
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Phycocyanobilin
Phycocyanobilin is a blue phycobilin, i.e., a tetrapyrrole chromophore found in cyanobacteria and in the chloroplasts of red algae, glaucophytes, and some cryptomonads. Phycocyanobilin is present only in the phycobiliproteins allophycocyanin and phycocyanin, of which it is the terminal acceptor of energy. It is covalently linked to these phycobiliproteins by a thioether In organic chemistry, an organic sulfide (British English sulphide) or thioether is an organosulfur functional group with the connectivity as shown on right. Like many other sulfur-containing compounds, volatile sulfides have foul odors. A su ... bond. Phycocyanobilin, PCB, has the ability to bind to human serum albumin, HSA, protein found mainly in the blood of humans. This PCB-HCA complex benefits the structure of HSA, increasing the thermal stability of HSA, as well as increasing its ability to prevent against proteolytic activity of other proteins. References Further reading * Photosynt ...
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Phycoerythrobilin
Phycoerythrobilin is a red phycobilin, i.e. an open tetrapyrrole chromophore found in cyanobacteria and in the chloroplasts of red algae, glaucophytes and some cryptomonads. Phycoerythrobilin is present in the phycobiliprotein phycoerythrin, of which it is the terminal acceptor of energy. The amount of phycoerythrobilin in phycoerythrins varies a lot, depending on the considered organism. In some Rhodophytes and oceanic cyanobacteria, phycoerythrobilin is also present in the phycocyanin Phycocyanin is a pigment-protein complex from the light-harvesting phycobiliprotein family, along with allophycocyanin and phycoerythrin. It is an accessory pigment to chlorophyll. All phycobiliproteins are water-soluble, so they cannot exist wi ..., then termed R-Phycocyanin. Like all phycobilins, phycoerythrobilin is covalently linked to these phycobiliproteins by a thioether bond. References * External links Chemical Structure of phycoerythrobilin {{Tetrapyrroles Tetrapyrroles Photosy ...
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Phycourobilin
Phycourobilin is an orange tetrapyrrole involved in photosynthesis in cyanobacteria and red algae. This chromophore is bound to the phycobiliprotein phycoerythrin, the distal component of the light-harvesting system of cyanobacteria and red algae (phycobilisome). When bound to phycoerythrin, phycourobilin shows an absorption maximum around 495 nm. This chromophore is always a donor chromophore of phycoerythrins, since their acceptor chromophore is always phycoerythrobilin. It can also be linked to the linker polypeptides of the phycobilisome, in which its precise role remains unclear. Phycourobilin is found in marine phycobilisome containing organisms, allowing them to efficiently absorb blue-green light. In the ubiquitous marine cyanobacteria ''Synechococcus ''Synechococcus'' (from the Greek ''synechos'', in succession, and the Greek ''kokkos'', granule) is a unicellular cyanobacterium that is very widespread in the marine environment. Its size varies from 0.8 to 1.5 µ ...
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Chlorophyll
Chlorophyll (also chlorophyl) is any of several related green pigments found in cyanobacteria and in the chloroplasts of algae and plants. Its name is derived from the Greek words , ("pale green") and , ("leaf"). Chlorophyll allow plants to absorb energy from light. Chlorophylls absorb light most strongly in the blue portion of the electromagnetic spectrum as well as the red portion. Conversely, it is a poor absorber of green and near-green portions of the spectrum. Hence chlorophyll-containing tissues appear green because green light, diffusively reflected by structures like cell walls, is less absorbed. Two types of chlorophyll exist in the photosystems of green plants: chlorophyll ''a'' and ''b''. History Chlorophyll was first isolated and named by Joseph Bienaimé Caventou and Pierre Joseph Pelletier in 1817. The presence of magnesium in chlorophyll was discovered in 1906, and was that element's first detection in living tissue. After initial work done by German chemi ...
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Tetrapyrrole
Tetrapyrroles are a class of chemical compounds that contain four pyrrole or pyrrole-like rings. The pyrrole/pyrrole derivatives are linked by ( =- or -- units), in either a linear or a cyclic fashion. Pyrroles are a five-atom ring with four carbon atoms and one nitrogen atom. Tetrapyrroles are common cofactors in biochemistry and their biosynthesis and degradation feature prominently in the chemistry of life. Some tetrapyrroles form the active core of compounds with crucial biochemical roles in living systems, such as hemoglobin and chlorophyll. In these two molecules, in particular, the pyrrole macrocycle ring frames a metal atom, that forms a coordination compound with the pyrroles and plays a central role in the biochemical function of those molecules. Structure Linear tetrapyrroles (called bilanes) include: *Heme breakdown products (e.g., bilirubin, biliverdin) * Phycobilins (found in cyanobacteria) *Luciferins as found in dinoflagellates and euphausiid shrimps (krill) F ...
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Water Column
A water column is a conceptual column of water from the surface of a sea, river or lake to the bottom sediment.Munson, B.H., Axler, R., Hagley C., Host G., Merrick G., Richards C. (2004).Glossary. ''Water on the Web''. University of Minnesota-Duluth. Retrieved 27 May 2014. Descriptively, the deep sea water column is divided into five parts—'' pelagic zones'' (from Greek πέλαγος (pélagos), 'open sea')—from the surface to below the floor, as follows: ''epipelagic'', from the surface to 200 meters below the surface; ''mesopelagic'', from 200 to 1000 meters below the surface; '' bathypelagic'', from 1000 to 4000 meters below the surface; ''abyssopelagic'', from 4000 meters below the surface to the level sea floor; ''hadopelagic'', depressions and crevices below the level sea floor. The concept of water column is useful since many aquatic phenomena are explained by the incomplete vertical mixing of waters with discrete chemical, physical or biological characteristics. Fo ...
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Stopping Power (particle Radiation)
In nuclear and materials physics, stopping power is the retarding force acting on charged particles, typically alpha and beta particles, due to interaction with matter, resulting in loss of particle kinetic energy. Its application is important in areas such as radiation protection, ion implantation and nuclear medicine.ICRU Report 73: Stopping of Ions heavier than Helium, Journal of the ICRU, 5 No. 1 (2005), Oxford Univ. Press Definition and Bragg curve Both charged and uncharged particles lose energy while passing through matter. Positive ions are considered in most cases below. The stopping power depends on the type and energy of the radiation and on the properties of the material it passes. Since the production of an ion pair (usually a positive ion and a (negative) electron) requires a fixed amount of energy (for example, 33.97 eV in dry air), the number of ionizations per path length is proportional to the stopping power. The ''stopping power'' of the material is numeric ...
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