Oxyluciferin fluorescence is a model of native bioluminescence in the firefly luciferin—luciferase system

Gandelman, Olga; Brovko, Lubov; Ugarova, N. N.; Chikishev, A. Yu.; Shkurimov, A.P.

doi:10.1016/1011-1344(93)87083-y

Cited by 81 publications

(113 citation statements)

References 18 publications

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“…An excited oxyluciferin molecule deactivates in a water microenvironment with the emission of a light quantum and binds again with the enzyme, thus forming an enzyme-product complex. The experimental facts that the rotational correlation time of luciferin in the complex with luciferase almost equals that in an aqueous solution 9 and the spectral parameters of bioluminescence are the most close to that of an oxyluciferin aqueous solution 10 are consistent with this hypothesis.…”

Section: Introductionsupporting

confidence: 59%

Transient increase of tryptophan fluorescence of enzyme caused by photoexcitation of ligand in luciferase-luciferin complex

et al. 1999

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Section: Introductionsupporting

confidence: 59%

Transient increase of tryptophan fluorescence of enzyme caused by photoexcitation of ligand in luciferase-luciferin complex

et al. 1999

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“…Deactivation of the latter is accompanied by emission of a quantum of light. The emitter structure in firefly bioluminescence was confirmed by investigation of oxyluciferin fluorescence properties in different model systems (3). Yellow-green fluorescence ( max = 560 nm) prevails for oxyluciferin at pH !…”

Section: Introductionmentioning

confidence: 94%

“…In the second step an acid anhydride (2) between the carboxylic group and AMP is formed, with the release of pyrophosphate. Through several intermediate stages, this anhydride is oxidized by oxygen, producing the cyclic peroxide, dioxytanone (3). Decarboxylation of this peroxide leads to formation of oxyluciferin in a singlet electronically excited state.…”

Section: Introductionmentioning

confidence: 99%

Protein structure and bioluminescent spectra for firefly bioluminescence

2002

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Modern theory on general and specific effects of microenvironment on emission spectra was used for explanation of spectral differences for both natural and mutant forms of beetle luciferases, as well as for bioluminescence emitter oxyluciferin in model systems. For the analysis, both authors' and other published data were used. It was shown that active site mutations that resulted in spectral shifts of bioluminescence as a rule caused substantial decrease in the catalytic activity of the enzyme. At the same time, mutations in the conservative regions of the protein amino acid sequence that were in the periphery of the protein globe resulted in red shift of the bioluminescence spectra without affecting catalytic activity. Correlation was observed between the value of spectral shift and polarizability of the introduced amino acid residue: the higher the polarizability, the larger was the red shift of bioluminescence.

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“…That is, the deprotonated forms of luciferin and ATP are expected to be the main species in the reaction mixture. 8,9 Consequently, the effective local concentration of luciferin and ATP at the positive surface of the cationic VET 1000 is greater than their stoichiometric concentrations in bulk water alone. Thus, the rate of the BL reaction could be greater in the solution containing the cationic VET 10000 than in water alone, resulting in the increase of the BL intensity in the presence of the cationic VET 1000 .…”

Section: Effect Of Membrane Surface Potential Of the Vet 1000 On The mentioning

confidence: 99%

Enhancement of Firefly Bioluminescence Using Liposomes Containing Cationic Components

et al. 1998

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An assay of adenosine 5′-triphosphate (ATP) is important to estimate the total amount of living cellar material (biomass) as well as the activity or metabolic state of the cells, since all types of living cells use ATP for storage of energy produced via metabolic processes. The firefly bioluminescence (BL) method has been widely used for the determination of ATP. In the firefly luciferin-luciferase reaction, luciferase catalyses the oxidative decarboxylation of luciferin in the presence of ATP and Mg 2+ , with concomitant BL:Firefly BL provides a rapid and very sensitive method for the determination of ATP. 1 Recently, the enhancement of light emission has been noted in view of improving the sensitivity of the firefly BL assay for ATP. The presence of apporopriate aqueous micellar media can increase the maximum BL intensity. Aqueous nonionic and zwitterionic micellar media increased the BL peak height intensity as well as prolonged the dulation of the BL.2 In addition, cationic detergents such as benzalkonium chloride increased the firefly luciferin-luciferase reaction rate several-fold, with a sharply defined optimum concentration of detergent. 3 However, the enhancement of light emission in the presence of surfactant micelles was observed only when higher ATP concentrations were used. luciferin+ATP+Mg 2+ +O2 → oxyluciferin+AMP+PPi+CO2+light luciferase Previously, we found that a cationic polysaccharide such as diethylaminoethyl dextran was more effective than other types of charged polysaccharides in enhancing the BL intensity. 4 The detection limit for ATP was improved by a factor of three times compared to that in water alone. In addition, the effect of different chargetypes of liposome on the BL intensity was investigated.5 Cationic liposome containing stearylamine (SA) was superior to anionic and zwitterionic liposomes as an enhancer in the firefly luciferinluciferase BL reaction. The sensitivity for ATP in the presence of cationc liposome containing SA was improved by a factor of five times compared to that in water alone.The aim of this work was to prepare newly cationic liposomes using stearyltrimethylammonium chloride and tetracaine as a cationic component for improving the sensitivity of firefly BL assay for ATP and to clarify the differences in the BL enhancement between cationic components by measuring membrane surface potential of the cationic liposomes. Experimental MaterialsLuciferase from firefly (Photinus pyralis: product number L9009), D-luciferin, The effect of cationic components in liposome on the bioluminescence (BL) intensity from the firefly luciferin-luciferase reaction with ATP was investigated by use of vesicles formed by the extrusion technique (VET). Stearyltrimethylammonium chloride (STAC), stearylamine (SA) and tetracaine (TC) were used as cationic components. The VET containing STAC and SA enhanced the maximum BL intensity. In contrast, a lowering of the maximum BL intensity was observed in the presence of the VET containing TC. The sensitivity for ATP in the presence o...

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Oxyluciferin fluorescence is a model of native bioluminescence in the firefly luciferin—luciferase system

Cited by 81 publications

References 18 publications

Transient increase of tryptophan fluorescence of enzyme caused by photoexcitation of ligand in luciferase-luciferin complex

Transient increase of tryptophan fluorescence of enzyme caused by photoexcitation of ligand in luciferase-luciferin complex

Protein structure and bioluminescent spectra for firefly bioluminescence

Enhancement of Firefly Bioluminescence Using Liposomes Containing Cationic Components

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