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Luciferin
Luciferin (from the Latin ''lucifer'', "light-bearer") is a generic term for the light-emitting compound found in organisms that generate bioluminescence. Luciferins typically undergo an enzyme-catalyzed reaction with molecular oxygen. The resulting transformation, which usually involves splitting off a molecular fragment, produces an excited state intermediate that emits light upon decaying to its ground state. The term may refer to molecules that are substrates for both luciferases and photoproteins. Types Luciferins are a class of small-molecule substrates that react with oxygen in the presence of a luciferase (an enzyme) to release energy in the form of light. It is not known just how many types of luciferins there are, but some of the better-studied compounds are listed below. Because of the chemical diversity of luciferins, there is no clear unifying mechanism of action, except that all require molecular oxygen, The variety of luciferins and luciferases, their diverse ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Luciferin Latia
Luciferin (from the Latin ''lucifer'', "light-bearer") is a generic term for the light-emitting compound found in organisms that generate bioluminescence. Luciferins typically undergo an enzyme-catalyzed reaction with molecular oxygen. The resulting transformation, which usually involves splitting off a molecular fragment, produces an excited state intermediate that emits light upon decaying to its ground state. The term may refer to molecules that are substrates for both luciferases and photoproteins. Types Luciferins are a class of small-molecule substrates that react with oxygen in the presence of a luciferase (an enzyme) to release energy in the form of light. It is not known just how many types of luciferins there are, but some of the better-studied compounds are listed below. Because of the chemical diversity of luciferins, there is no clear unifying mechanism of action, except that all require molecular oxygen, The variety of luciferins and luciferases, their diverse r ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Luciferin Bacterial
Luciferin (from the Latin ''lucifer'', "light-bearer") is a generic term for the light-emitting compound found in organisms that generate bioluminescence. Luciferins typically undergo an enzyme-catalyzed reaction with molecular oxygen. The resulting transformation, which usually involves splitting off a molecular fragment, produces an excited state intermediate that emits light upon decaying to its ground state. The term may refer to molecules that are substrates for both luciferases and photoproteins. Types Luciferins are a class of small-molecule substrates that react with oxygen in the presence of a luciferase (an enzyme) to release energy in the form of light. It is not known just how many types of luciferins there are, but some of the better-studied compounds are listed below. Because of the chemical diversity of luciferins, there is no clear unifying mechanism of action, except that all require molecular oxygen, The variety of luciferins and luciferases, their diverse r ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Firefly Luciferin
Firefly luciferin (also known as beetle luciferin) is the luciferin, or light-emitting compound, used for the firefly (Lampyridae), railroad worm ( Phengodidae), starworm ( Rhagophthalmidae), and click-beetle (Pyrophorini) bioluminescent systems. It is the substrate of luciferase ( EC 1.13.12.7), which is responsible for the characteristic yellow light emission from many firefly species. As with all other luciferins, oxygen is required to elicit light; however, it has also been found adenosine triphosphate (ATP) and magnesium are required for light emission. History Much of the early work on the chemistry of the firefly luminescence was done in the lab of William D. McElroy at Johns Hopkins University. The luciferin was first isolated and purified in 1949, though it would be several years until a procedure was developed to crystallize the compound in high yield. This, along with the synthesis and structure elucidation, was accomplished by Dr. Emil H. White at the Johns Hopkins ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Bioluminescence
Bioluminescence is the production and emission of light by living organisms. It is a form of chemiluminescence. Bioluminescence occurs widely in marine vertebrates and invertebrates, as well as in some fungi, microorganisms including some bioluminescent bacteria, and terrestrial arthropods such as fireflies. In some animals, the light is bacteriogenic, produced by symbiotic bacteria such as those from the genus '' Vibrio''; in others, it is autogenic, produced by the animals themselves. In a general sense, the principal chemical reaction in bioluminescence involves a light-emitting molecule and an enzyme, generally called luciferin and luciferase, respectively. Because these are generic names, luciferins and luciferases are often distinguished by the species or group, e.g. firefly luciferin. In all characterized cases, the enzyme catalyzes the oxidation of the luciferin. In some species, the luciferase requires other cofactors, such as calcium or magnesium ions, and so ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Luciferase
Luciferase is a generic term for the class of oxidative enzymes that produce bioluminescence, and is usually distinguished from a photoprotein. The name was first used by Raphaël Dubois who invented the words '' luciferin'' and ''luciferase'', for the substrate and enzyme, respectively. Both words are derived from the Latin word ''lucifer'', meaning "lightbearer", which in turn is derived from the Latin words for "light" (''lux)'' and "to bring or carry" (''ferre)''.Luciferases are widely used in biotechnology, for bioluminescence imaging microscopy and as reporter genes, for many of the same applications as fluorescent proteins. However, unlike fluorescent proteins, luciferases do not require an external light source, but do require addition of luciferin, the consumable substrate. Examples A variety of organisms regulate their light production using different luciferases in a variety of light-emitting reactions. The majority of studied luciferases have been found in an ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Latia Neritoides
''Latia neritoides'' is a species of small freshwater snail or limpet, an aquatic gastropod mollusc in the family Latiidae. The type specimen is in the British Museum. The specific epithet "neritoides" means "like a nerite". The shell of this species has an internal shelf or lamella, but it more closely resembles a shell of a '' Crepidula'' than it does a ''Nerita''. Distribution This species is endemic to the North Island of New Zealand. Habitat This limpet lives in clean running streams and rivers. Powell A. W. B., ''New Zealand Mollusca'', William Collins Publishers Ltd, Auckland, New Zealand 1979 Shell description The length of the shell is up to 11 mm. The width of the shell is up to 8 mm. The height of the shell is up to 4.5 mm. If the length of the shell is 8.5 mm, the width of the shell is 6 mm. The height of the shell is 3 mm. The shell is semiovate, thin and fragile, almost smooth, brown, semitransparent. Sculpture consisting of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Coelenterazine
Coelenterazine is a luciferin, a molecule that emits light after reaction with oxygen, found in many aquatic organisms across eight phyla. It is the substrate of many luciferases such as '' Renilla reniformis'' luciferase (Rluc), ''Gaussia'' luciferase (Gluc), and photoproteins, including aequorin, and obelin. All these proteins catalyze the oxidation of this substance, a reaction catalogued EC 1.13.12.5. History Coelenterazine was simultaneously isolated and characterized by two groups studying the luminescent organisms sea pansy (''Renilla reniformis'') and the cnidarian ''Aequorea victoria'', respectively. Both groups independently discovered that the same compound was used in both luminescent systems. The molecule was named after the now-obsolete phylum coelenterata. Likewise, the two main metabolites – coelenteramide and coelenteramine – were named after their respective functional groups. While coelenterazine was first discovered in ''Aequorea victoria'', it was later ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Fatty Aldehyde
Fatty aldehydes are aliphatic, long-chain aldehydes which may be mono- or polyunsaturated. The fatty aldehydes include compounds such as octanal, nonanal, decanal or dodecanal. The nomenclature is derived from the nomenclature of the alkanes, the ending ''-al'' is added to indicate the aldehyde group. Occurrence Fatty aldehydes are a natural component of many natural ingredients such as the essential oils of various citrus fruits. Decanal, for example, is a component of orange peel. The pheromone cocktails of various insect pheromones contain fatty aldehydes. Fat aldehydes were also detected in the heart muscle of mammals. Preparation Fatty aldehydes can be prepared by dehydrogenation of fatty alcohols on copper-zinc catalysts. By the hydroformylation of alkenes, fatty aldehydes are produced on a large industrial scale. Use A large proportion of the fatty aldehydes prepared by hydroformylation is directly processed further to fatty alcohols. Many fatty aldehydes find use ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Flavin Mononucleotide
Flavin mononucleotide (FMN), or riboflavin-5′-phosphate, is a biomolecule produced from riboflavin (vitamin B2) by the enzyme riboflavin kinase and functions as the prosthetic group of various oxidoreductases, including NADH dehydrogenase, as well as cofactor in biological blue-light photo receptors. During the catalytic cycle, a reversible interconversion of the oxidized (FMN), semiquinone (FMNH•), and reduced (FMNH2) forms occurs in the various oxidoreductases. FMN is a stronger oxidizing agent than NAD and is particularly useful because it can take part in both one- and two-electron transfers. In its role as blue-light photo receptor, (oxidized) FMN stands out from the 'conventional' photo receptors as the signaling state and not an E/Z isomerization. It is the principal form in which riboflavin is found in cells and tissues. It requires more energy to produce, but is more soluble than riboflavin. In cells, FMN occurs freely circulating but also in several covalently bou ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Bioluminescent Bacteria
Bioluminescent bacteria are light-producing bacteria that are predominantly present in sea water, marine sediments, the surface of decomposing fish and in the gut of marine animals. While not as common, bacterial bioluminescence is also found in terrestrial and freshwater bacteria. These bacteria may be free living (such as ''Vibrio harveyi'') or in symbiosis with animals such as the Hawaiian Bobtail squid (''Aliivibrio fischeri'') or terrestrial nematodes (''Photorhabdus luminescens''). The host organisms provide these bacteria a safe home and sufficient nutrition. In exchange, the hosts use the light produced by the bacteria for camouflage, prey and/or mate attraction. Bioluminescent bacteria have evolved symbiotic relationships with other organisms in which both participants benefit close to equally. Another possible reason bacteria use luminescence reaction is for quorum sensing, an ability to regulate gene expression in response to bacterial cell density. History Records o ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
