Stereospecificity and Firefly Bioluminescence, a Comparison of Natural and Synthetic Luciferins

Seliger, H. H.; McElroy, W. D.; White, Emil H.; Field, George F.

doi:10.1073/pnas.47.8.1129

Cited by 76 publications

(54 citation statements)

References 7 publications

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“…The L-LH 2 isomer can also be adenylylated, giving rise to L-LH 2 -AMP; however it is not used further in light production (24,27). …”

Section: Firefly Luciferase Reactionsmentioning

confidence: 99%

“…For a long time D-LH 2 was regarded as the only isomer capable of producing light (14,27), the L-LH 2 isomer behaving as an inhibitor (46,47,57), although both D-and L-isomer can be adenylylated by luciferase. Through a mechanism analogous to its synthesis the added L-LH 2 would be adenylylated, converted to L-LH 2 -CoA and then racemized and hydrolyzed to D-LH 2 .…”

Section: Firefly Luciferin Biosynthesis and The Stereo-specificity Inmentioning

confidence: 99%

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Firefly bioluminescence: A mechanistic approach of luciferase catalyzed reactions

2008

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SummaryLuciferase is a general term for enzymes catalyzing visible light emission by living organisms (bioluminescence). The studies carried out with Photinus pyralis (firefly) luciferase allowed the discovery of the reaction leading to light production. It can be regarded as a two-step process: the first corresponds to the reaction of luciferase's substrate, luciferin (LH 2 ), with ATPMg 21 generating inorganic pyrophosphate and an intermediate luciferyl-adenylate (LH 2 -AMP); the second is the oxidation and decarboxylation of LH 2 -AMP to oxyluciferin, the light emitter, producing CO 2 , AMP, and photons of yellow-green light (550-570 nm). In a dark reaction LH 2 -AMP is oxidized to dehydroluciferyl-adenylate (L-AMP). Luciferase also shows acyl-coenzyme A synthetase activity, which leads to the formation of dehydroluciferyl-coenzyme A (L-CoA), luciferyl-coenzyme A (LH 2 -CoA), and fatty acyl-CoAs. Moreover luciferase catalyzes the synthesis of dinucleoside polyphosphates from nucleosides with at least a 3 0 -phosphate chain plus an intact terminal pyrophosphate moiety. The LH 2 stereospecificity is a particular feature of the bioluminescent reaction where each isomer, D-LH 2 or L-LH 2 , has a specific function. Practical applications of the luciferase system, either in its native form or with engineered proteins, encloses the analytical assay of metabolites like ATP and molecular biology studies with luc as a reporter gene, including the most recent and increasing field of bioimaging.2008 IUBMB IUBMB Life, 61(1):

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“…The L-LH 2 isomer can also be adenylylated, giving rise to L-LH 2 -AMP; however it is not used further in light production (24,27). …”

Section: Firefly Luciferase Reactionsmentioning

confidence: 99%

Section: Firefly Luciferin Biosynthesis and The Stereo-specificity Inmentioning

confidence: 99%

Firefly bioluminescence: A mechanistic approach of luciferase catalyzed reactions

2008

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“…L-Luciferin is an enantiomer of D-luciferin and was synthesized in order to identify the chemical structure of natural D-luciferin [25]. In the standard reaction mixtures, L-luciferin is not used in the luminescence reaction [25].…”

Section: Firefly Luciferin = D(-)-luciferin (D-lh 2 )mentioning

confidence: 99%

“…In the standard reaction mixtures, L-luciferin is not used in the luminescence reaction [25]. L-Luciferin is a potent competitive inhibitor of luciferase and the K i value is between 3 and 4 lM [26].…”

Section: Firefly Luciferin = D(-)-luciferin (D-lh 2 )mentioning

confidence: 99%

Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions

Inouye

2009

Cell. Mol. Life Sci.

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Firefly luciferase is a member of the acyl-adenylate/thioester-forming superfamily of enzymes and catalyzes the oxidation of firefly luciferin with molecular oxygen to emit light. Knowledge of the luminescence mechanism catalyzed by firefly luciferase has been gathered, leading to the discovery of a novel catalytic function of luciferase. Recently, we demonstrated that firefly luciferase has a catalytic function of fatty acyl-CoA synthesis from fatty acids in the presence of ATP, Mg(2+) and coenzyme A. Based on identification of fatty acyl-CoA genes in firefly, Drosophila, and non-luminous click beetles, we then proposed that the evolutionary origin of firefly luciferase is a fatty acyl-CoA synthetase in insects. Further, we succeeded in converting the fatty acyl-CoA synthetase of non-luminous insects into functional luciferase showing luminescence activity by site-directed mutagenesis.

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“…L-Luciferin is not a substrate for the bioluminescence reaction, 15) and Niwa et al 12) suggested that the larva of L. lateralis possesses approximately 1:1 mixture of D-and L-luciferin by an HPLC analysis using a chiral column. In our analysis, the content of luciferin in the larva of L. lateralis measured by HPLC analysis was larger than that by the L-L reaction analysis (although statistically not significant; Table 1).…”

Section: )mentioning

confidence: 99%