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Biliprotein
Biliproteins are pigment protein compounds that are located in photosynthesising organisms such as algae, and sometimes also in certain insects. They refer to any protein that contains a bilin chromophore. In plants and algae, the main function of biliproteins is to make the process of light accumulation required for photosynthesis more efficient; while in insects they play a role in growth and development. Some of their properties: including light-receptivity, light-harvesting and fluorescence have made them suitable for applications in bioimaging and as indicators; while other properties such as anti-oxidation, anti-aging and anti-inflammation in phycobiliproteins have given them potential for use in medicine, cosmetics and food technology. While research on biliproteins dates back as far as 1950, it was hindered due to issues regarding biliprotein structure, lack of methods available for isolating individual biliprotein components, as well as limited information on lyase react ...
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Bilin (biochemistry)
Bilins, bilanes or bile pigments are biological pigments formed in many organisms as a metabolic product of certain porphyrins. Bilin (also called bilichrome) was named as a bile pigment of mammals, but can also be found in lower vertebrates, invertebrates, as well as red algae, green plants and cyanobacteria. Bilins can range in color from red, orange, yellow or brown to blue or green. In chemical terms, bilins are linear arrangements of four pyrrole rings (tetrapyrroles). In human metabolism, bilirubin is a breakdown product of heme. A modified bilane is an intermediate in the biosynthesis and uroporphyrinogen III from porphobilinogen. Examples of bilins are found in animals (cardinal examples are bilirubin and biliverdin), and phycocyanobilin, the chromophore of the photosynthetic pigment phycocyanin, in algae and plants. In plants, bilins also serve as the photopigments of the photoreceptor protein phytochrome. An example of an invertebrate bilin is micromatabilin, whic ...
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Manduca Sexta
''Manduca sexta'' is a moth of the family Sphingidae present through much of the Americas. The species was first described by Carl Linnaeus in his 1763 ''Centuria Insectorum''. Commonly known as the Carolina sphinx moth and the tobacco hawk moth (as adults) and the tobacco hornworm and the Goliath worm (as larvae), it is closely related to and often confused with the very similar tomato hornworm (''Manduca quinquemaculata''); the larvae of both feed on the foliage of various plants of the family Solanaceae. The larvae of these species can be distinguished by their lateral markings: Tomato hornworms have eight V-shaped white markings with no borders; tobacco hornworms have seven white diagonal lines with a black border. Additionally, tobacco hornworms have red horns, while tomato hornworms have dark blue or black horns. A mnemonic to remember the markings is tobacco hornworms have straight white lines like cigarettes, while tomato hornworms have V-shaped markings (as in "vine-ri ...
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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 Cryptomonad, 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 Protein quaternary structure, trim ...
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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 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 convention ...
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Cryptomonad
The cryptomonads (or cryptophytes) are a superclass of algae, most of which have plastids. They are traditionally considered a division of algae among phycologists, under the name of Cryptophyta. They are common in freshwater, and also occur in marine and brackish habitats. Each cell is around 10–50 μm in size and flattened in shape, with an anterior groove or pocket. At the edge of the pocket there are typically two slightly unequal flagella. Some may exhibit mixotrophy. They are classified as superclass Cryptomonada, which is divided into two classes: heterotrophic Goniomonadea and phototrophic Cryptophyceae. The two groups are united under three shared morphological characteristics: presence of a periplast, ejectisomes with secondary scroll, and mitochondrial cristae with flat tubules. Genetic studies as early as 1994 also supported the hypothesis that ''Goniomonas'' was sister to Cryptophyceae. A study in 2018 found strong evidence that the common ancestor of Crypto ...
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Red Algae
Red algae, or Rhodophyta (, ; ), make up one of the oldest groups of eukaryotic algae. The Rhodophyta comprises one of the largest Phylum, phyla of algae, containing over 7,000 recognized species within over 900 Genus, genera amidst ongoing taxonomic revisions. The majority of species (6,793) are Florideophyceae, and mostly consist of multicellular, ocean, marine algae, including many notable seaweeds. Red algae are abundant in marine habitats. Approximately 5% of red algae species occur in freshwater environments, with greater concentrations in warmer areas. Except for two coastal cave dwelling species in the asexual class Cyanidiophyceae, no terrestrial species exist, which may be due to an evolutionary bottleneck in which the last common ancestor lost about 25% of its core genes and much of its evolutionary plasticity. Red algae form a distinct group characterized by eukaryotic cells without flagella and centrioles, chloroplasts without external endoplasmic reticulum or unstack ...
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Cyanobacteria
Cyanobacteria ( ) are a group of autotrophic gram-negative bacteria that can obtain biological energy via oxygenic photosynthesis. The name "cyanobacteria" () refers to their bluish green (cyan) color, which forms the basis of cyanobacteria's informal common name, blue-green algae. Cyanobacteria are probably the most numerous taxon to have ever existed on Earth and the first organisms known to have produced oxygen, having appeared in the middle Archean eon and apparently originated in a freshwater or terrestrial environment. Their photopigments can absorb the red- and blue-spectrum frequencies of sunlight (thus reflecting a greenish color) to split water molecules into hydrogen ions and oxygen. The hydrogen ions are used to react with carbon dioxide to produce complex organic compounds such as carbohydrates (a process known as carbon fixation), and the oxygen is released as a byproduct. By continuously producing and releasing oxygen over billions of years, cyanobacte ...
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Phycobilisome
Phycobilisomes are light-harvesting antennae that transmit the energy of harvested photons to photosystem II and photosystem I in cyanobacteria and in the chloroplasts of red algae and glaucophytes. They were lost during the evolution of the chloroplasts of green algae and plants. 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 phyco ...
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Methine Group
In organic chemistry, a methine group or methine bridge is a trivalent functional group , derived formally from methane. It consists of a carbon atom bound by two single bonds and one double bond, where one of the single bonds is to a hydrogen. The group is also called methyne or methene, but its IUPAC systematic name is methylylidene or methanylylidene. This group is sometimes called "methylidyne", however that name belongs properly to either the methylidyne group (connected to the rest of the molecule by a triple bond) or to the methylidyne radical (the two atoms as a free molecule with dangling bonds). The name "methine" is also widely used in non-systematic nomenclature for the methanetriyl group (IUPAC): a carbon atom with four single bonds, where one bond is to a hydrogen atom (). (2007''Methanetriyl group''in the Chemical Entities of Biological Interest (ChEBI) database. Accessed on 2015-03-05. Overlapping methines Two or more methine bridges can overlap, forming a ...
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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 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. Biosynthetic Pathway The biosynthetic pathway of phycocyanobilin begins with 5-Aminolevulinic acid (5-ALA). Two molecules of 5-ALA undergo a condensation reaction catalyzed by Porphobilinogen (PBG) Synthase to yield a molecule of Porphobilinogen (PBG) (not shown). Four molecules of PBG are polymerized ...
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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 ..., 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 Photosynthetic pigment ...
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