Luciferin aldehyde

The formation of aldehydes from 1,1-disubstituted epoxides has occasionally found use in synthesis, although simpler aldehydes in particular tend to form dioxolane dimers by BFs-induced reaction with epoxide. Hill et a converted the epoxide (94), which had been prepared from a 3-ionone derivative, into luciferin aldehyde (95) by treatment with cold BF3 etherate (equation 38). 

Properties of Latia luciferin. Latia luciferin is a highly hydrophobic, fat-soluble compound, and volatile under vacuum. It is a colorless liquid, with an absorption maximum at 207nm (s approx. 13,700 Fig. 6.1.2). The chemical structure of Latia luciferin has been determined to be 1 (C15H24O2), an enol formate of a terpene aldehyde 3 (Fig. 6.1.3 Shimomura and Johnson, 1968b). The enol formate group of Latia luciferin is unstable the luciferin is spontaneously hydrolyzed... 

When an excess amount of luciferin was preincubated with H2O2 before the addition of luciferase, the quantum yields of luciferase and the luciferin-H202 adduct were found to be 0.63 and 0.03, respectively (Rudie et al., 1981). The aldehyde group of luciferin is probably converted into the corresponding acid in the luminescence reaction, although it has not been experimentally confirmed. 

Mild chromic acid oxidation of luciferin (CrOs/KHSC /HiO, room temperature) yielded 3-methyl-4-vinylmaleimide (1, Fig. 8.7), 3-methyl-4-ethylmaleimide (2), and an aldehyde (3), whereas vigorous chromic acid oxidation (CrOs/2N H2SO4, 90°C) gave hema-tinic acid (4) (Dunlap et al., 1981). These results closely resemble the results of the chromic acid oxidation of the fluorescent compound F of euphausiid (p. 76), indicating a structural similarity between dinoflagellate luciferin and the compound F. 

Exchange of oxygen atom between the C=0 group of luciferin and the solvent water. The exchange is slow with carboxylic acids but fairly rapid with aldehydes and ketones (Samuel, 1962). 

Strehler, B. L., and Cormier, M. J. (1954). Isolation, identification, and function of long chain fatty aldehydes affecting the bacterial luciferin-luciferase reaction. J. Biol. Chem. 211 213-225. 

Quantula (Dyakia), 180, 334 Quantum yield, xvi, 361, 362 aequorin, 104, 106, 110 aldehydes in bacterial bioluminescence, 36, 41 Chaetopterus photoprotein, 224 coelenterazine, 85, 143, 149 Cypridina luciferin, 69-71 definition, xvi, 361 Diplocardia bioluminescence, 242 firefly luciferin, 12 fluorescent compound F, 73 Latia luciferin, 190 pholasin, 197 PMs, 286... 

Discovery of luciferin-luciferase reaction Benzoylation of Cypridina luciferin ATP requirement in firefly luminescence Requirement for long-chain aldehyde (luciferin) in bacterial luminescence... 

The chapters in this book are arranged roughly in the chronological order of bioluminescence systems discovered, based on the date of the major breakthrough made in each bioluminescence system, such as the discovery of ATP in the firefly system (McElroy, 1947) and the identification of fatty aldehyde as the luciferin in luminous bacteria (Cormier and Strehler, 1953). This differs from Harvey s 1952 book, which is arranged in the order of taxonomic classification. 

The use of the fire fly light-emitting system. Light generation depends on the oxidation of a substance known as luciferin. This is a fatty aldehyde such as dodecanal. An enzyme called luciferase, extracted from fire flies, catalyses the oxidation. The reaction also requires ATP. Thus, light emission measures ATP. 

Oligochetes (earthworms) 500 Luciferine (an aldehyde), luciferase, h2o2... 

Figure 3 Luciferase-catalyzed bioluminescent reaction with (A) luciferin and (B) an aldehyde compound and FMNH2.

Some new luminescent and fluorescent reporters (some of them even non-substrate proteins ) are very attractive because of their easy and fast detection, explaining their current frequent use. The bacterial luciferase isolated from the Vibrio fischeri lux operon contains luxAB encoding the functional subunits and luxCDE for the synthesis and recycling of the aldehyde substrate (Prosser, 1996). Firefly (Photinus pyralis) luciferase, encoded by the luc gene catalyses the oxidative carboxylation of beetle luciferin, in which photons are emitted (LaRossa, 1998). Its short half-life and lack of any post-translational modification makes it ideal to look after effects in gene expression (Naylor, 1999). Detection of... 

The initial syntheses of Cypridina luciferin and its analogues were performed in low yields by reaction of appropriate 2-aminopyrazines with a-keto acids, followed by reduction with aluminum amalgam or catalytic hydrogenation, and treatment of the product with dicyclohexyl-carbodiimide. For example, 2-amino-5-phenylpyrazine (36) on reaction with pyruvic acid gave the product 37, which was reduced to give an intermediate formulated as 38, which was then cyclized to give the 0x0 compound 39 in 7% yield. It was later discovered that these products could be obtained in high yield in one step by reaction of aminopyrazines such as 36 with a-keto aldehydes such as pyruvaldehyde (MeCOCHO). Condensation of the appropriate aminopyrazine with... 

Although other luminescent systems have been studied (including those of the fireworm and the limpet, both of which use aldehydes as luciferins), bioluminescence remains somewhat mysterious. Elucidation of the chemical and biological bases for luminescence systems in other organisms should improve understanding of why the remarkable and beautiful phenomenon of bioluminescence appears in so many species, see also Chemiluminescence. 

If luminescence is a result of a biochemical reaction, the principle is called bioluminescence. The most frequently used bioluminescence system is that of the firefly. The enzyme luciferase catalyses the oxidation of luciferin as a substrate in the presence of adenosine triphosphate (ATP) (Scheme 7). Another bioluminescence system makes use of a luciferase from certain marine bacteria. A long-chain aldehyde is oxidized in the presence of luciferase, an oxido-reductase and NAD/NADH. Recently, a photoprotein isolated from the bioluminescent jellyfish Aequorea victoria, has been found to be an efficient bioluminescence label for immunoassays. 

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