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Oxyluciferin
Luciferin () 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 breaking 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 reaction mechanisms and the scattered phylo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Firefly Luciferase
Firefly luciferase is the light-emitting enzyme responsible for the bioluminescence of fireflies and click beetles. The enzyme catalyses the oxidation of firefly luciferin, requiring oxygen and ATP. Because of the requirement of ATP, firefly luciferases have been used extensively in biotechnology. Mechanism of reaction The chemical reaction catalyzed by firefly luciferase takes place in two steps: * luciferin + ATP → luciferyl adenylate + PPi * luciferyl adenylate + O2 → oxyluciferin + AMP + light Light is produced because the reaction forms oxyluciferin in an electronically excited state. The reaction releases a photon of light as oxyluciferin goes back to the ground state. Luciferyl adenylate can additionally participate in a side reaction with O2 to form hydrogen peroxide and dehydroluciferyl-AMP. About 20% of the luciferyl adenylate intermediate is oxidized in this pathway. Firefly luciferase generates light from luciferin in a multistep process. First, D-lu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Bioluminescence
Bioluminescence is the emission of light during a chemiluminescence reaction by living organisms. Bioluminescence occurs in multifarious organisms ranging from marine vertebrates and invertebrates, as well as in some Fungus, fungi, microorganisms including some bioluminescent bacteria, Dinoflagellate, dinoflagellates and terrestrial arthropods such as Firefly, fireflies. In some animals, the light is bacteriogenic, produced by symbiosis, symbiotic bacteria such as those from the genus ''Vibrio''; in others, it is autogenic, produced by the animals themselves. In most cases, the principal chemical reaction in bioluminescence involves the reaction of a substrate called luciferin and an enzyme, called luciferase. Because these are generic names, luciferins and luciferases are often distinguished by the species or group, e.g. firefly luciferin or Vargulin, cypridina luciferin. In all characterized cases, the enzyme Catalysis, catalyzes the Redox, oxidation of the luciferin resultin ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Photoprotein
Photoproteins are a type of enzyme produced by bioluminescent organisms. They add to the function of the luciferins whose usual light-producing reaction is catalyzed by the enzyme luciferase. History The term photoprotein was first used to describe the unusual chemistry of the luminescent system of ''Chaetopterus'' (a marine Polychaete worm). This was meant to distinguish them from other light-producing proteins because these do not exhibit the usual luciferin-luciferase reaction. Reaction kinetics Photoproteins do not display typical enzyme kinetics as seen in luciferases. Instead, when mixed with luciferin, they display luminescence proportional to the amount of the photoprotein. For example, the photoprotein aequorin produces a flash of light when luciferin and calcium are added, rather than the prolonged glow that is seen for luciferases when luciferin is added. In this respect, it may appear that photoproteins are not enzymes, when in fact they do catalyze their biolumines ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Firefly Luciferin
Firefly luciferin (also known as beetle luciferin) is the luciferin, precursor of the light-emitting compound, used for the firefly ( Lampyridae), railroad worm ( Phengodidae), starworm ( Rhagophthalmidae), and click-beetle ( Pyrophorini) bioluminescent systems. It is the substrate of firefly luciferase ( EC 1.13.12.7), which is responsible for the characteristic light emission of many firefly and other insect species in the visible spectra ranging from 530 until 630 nm. As with other luciferins, oxygen is essential for the luminescence mechanism, which involves the decomposition of a cyclic peroxide to produce excited-state molecules capable of emitting light as they relax to the ground state. Additionally, it has been found that 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 is ... [...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 u ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Flavin Mononucleotide V2
Flavin may refer to: Science * Flavin adenine dinucleotide (FAD), a redox cofactor * Flavin-containing amine oxidoreductase, a family of amine oxidases * Flavin-containing monooxygenase (FMO), a protein family * Flavin containing monooxygenase 1, a human gene * Flavin containing monooxygenase 3, a human gene * Flavin group, a group of organic compounds * Flavin mononucleotide, a biomolecule produced from riboflavin * Flavin reductase, an enzyme Places * Flavin, Aveyron, a commune in southern France People * Adrian Flavin (born 1979), a professional rugby player * Christopher Flavin, president of the Worldwatch Institute * Dan Flavin (1933–1996), a minimalist artist famous for using fluorescent light fixtures * Dan Flavin (politician), Louisiana politician * Dick Flavin (Gaelic footballer) (born 1978), Irish Gaelic football player * Dick Flavin (poet) (1936–2022), American poet * James Flavin (1906–1976), an American character actor * Jennifer Flavin (born 1968), a former ... [...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 a cofactor in biological blue-light photo receptors. During the catalytic cycle, various oxidoreductases induce reversible interconversions between the oxidized (FMN), semiquinone (FMNH•), and reduced (FMNH2) forms of the isoalloxazine core. 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 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Bioluminescent Bacteria
Bioluminescent bacteria are Bioluminescence, 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, 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 each other equally. Bacteria also use luminescence reaction for quorum sensing, an ability to regulate gene expression in response to bacterial cell density. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Luciferin Latia
Luciferin () 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 breaking 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 reaction mechanisms and the scattered phy ... [...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 wa ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
