Photinus pyralis

It has been suggested that the oxidation of Photinus pyralis luciferin (170) forms oxyluciferin (171) as the oxidized product (Scheme 88) (405-407), which was too unstable to be isolated and was rapidly converted in three other compounds. 

Fig. 1.7 Spectral change of the in vitro firefly bioluminescence by pH, with Photinus pyralis luciferase in glycylglycine buffer. The normally yellow-green luminescence (Amax 560 nm) is changed into red (Xmax 615 nm) in acidic medium, accompanied by a reduction in the quantum yield. From McElroy and Seliger, 1961, with permission from Elsevier.

The bioluminescence systems of Phengodidae (railroad worms) and Elateroidae (click beetles) are basically identical to that of Lampyridae (fireflies), requiring firefly luciferin, ATP, Mg2+ and a luciferase for light emission. However, there seem to be some differences. Viviani and Bechara (1995) reported that the spectra of the luminescence reactions measured with the luciferases of Brazilian fireflies (6 species) shift from the yellow-green range to the red range with lowering of the pH of the medium, like in the case of the Photinus pyralis luciferase (see Section 1.1.5), whereas the spectra... 

Although numerous luminous organisms are known, only a few of them has been studied and really exploited. Analytical applications of bioluminescence concern mainly the detection of ATP with the firefly luciferase and of NADH with some marine bacteria systems. Luciferase from the North American firefly, i.e., Photinus pyralis, has been extensively studied10-12 and afterwards, attention has been paid to the luciferase from Luciola mingrelica, i.e., the North Caucasus firefly13 15. 

The bioluminescence of the American firefly (Photinus pyralis) is certainly the best-known bioluminescent reaction, thanks to the work of Me Elroy and coworkers and E. H. White and his group (for references see P, p. 138, 6,168,169)) The substrate of this enzyme-catalyzed chemiluminescent oxidation is the benzothiazole derivative 107 (Photinus luciferin) which yields the ketone 109 in a decarboxylation reaction. The concept of a concerted cleavage of a dioxetane derivative has been applied to this reaction 170> (see Section II. C.). Recent experiments with 18C>2 have challenged this concept, as no 180-containing carbon dioxide was detected from the oxidation of 107 171>. 

The most popular system in mechanistic and model studies as well as in analytical applications (clinical, food, environmental) appears to be that of firefly luciferin and luciferin-type-related model luminescence [3, 5,23, 57], The luciferase from Photinus pyralis, Photinus luciferin 4-monooxygenase (ATP-hydrolyzing), EC 1.13, 12.7, is a hydrophobic enzyme that catalyzes the air oxidation of luciferin in the presence of ATP and magnesium ions to yield light emission ... 

Beside that of Photinus pyralis, other luciferases have been described in the literature such as those from Luciola cruciata, Luciola lateralis [122], and Luciola mingrelica. Among them luciferase from the latter one has been employed for analytical purposes [123],... 

A number of chemiluminescent reactions are known. The oxidation of 3-aminophthalhydrazide (luminol) has been studied extensively. " The emission resulting from the reaction of certain oxalic acid derivatives is another outstanding example. When chemiluminescence occurs in living organisms, it is called bioluminescence. The best known example is observed in the firefly Photinus pyralis. Many review articles have... 

Table 3.4.5 summarizes the advantages and drawbacks of the main reporter systems. Firefly luciferase (from Photinus pyralis lucFF gene)... 

The reporter gene is the luc operon from the firefly Photinus pyralis. This operon codes for an enzyme, luciferase, that catalyses the reaction between D-luciferin (the substrate), and oxygen, and requires ATP as a cofactor. This reaction produces the emission light that provides the measure of enzyme activity. The oxidation of one molecule of luciferin involves one ATP molecule and releases one photon (a stoichiometric reaction) (DeLuca and McElroy, 1974 Wood el al. 1989). The reaction can be summarized as follows ... 

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... 

COMPARISON OF KINETIC PROPERTIES OF FIREFLY LUCIFERASE FROM PHOTINUS PYRALIS AND LUCIOLA MINGREUCA... 

In this age of powerful computers, it is no longer even necessary to find analytical solution to differential equations. There are many software packages available that cany out numerical integration of differential equations followed by non-linear regression to fit the model and assess its quality by comparing with experimental data. In this study we have used a numerical integration approach to compare kinetic properties of Photinus pyralis and Luciola mingrelica firefly luciferases. 

Photinus pyralis firefly luciferase (PP) was obtained from Sigma, Luciola mingrelica firefly luciferase (LM) was isolated and purified according to. Time-course of bioluminescent reaction rate (v) was monitored as the intensity of light (I) in time according to equation 1 using a luminometer model 1251 (LKB Sweden). 

Bioluminescence serves as an excellent reporter system as a sensitive marker for microbial detection, as a real-time, non-invasive reporter for measuring gene expression and as a measure of intracellular biochemical function (cell viability). Most widely studied of the bioluminescence systems are those belonging to the luminous bacteria Vibrio sp.. Photobacterium sp. and Photorhabdus luminescens) and the firefly Photinus pyralis). While these systems have proved extremely versatile, there are caveats to their use limiting the array of applications they can be applied to. These caveats mainly surround the nature of the luciferase enzymes, and include temperature and pH stability. 

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