The Spectral Distribution of Firefly Light

Seliger, H. H.; Buck, John D.; Fastie, W. G.; McElroy, W. D.

doi:10.1085/jgp.48.1.95

Cited by 103 publications

(62 citation statements)

References 2 publications

(3 reference statements)

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“…In Table ! of the previous paper (1) and in the present Table I we have reported in addition to the peak intensity wavelength values, the full width at half-maximum intensity ( F W H M ) for each of the firefly emission spectra measured. The average F W H M is calculated to be 690A 4-44A.…”

Section: Plagiophthalamusmentioning

confidence: 91%

The Spectral Distribution of Firefly Light. II

Biggley

Lloyd

Seliger

1967

The Journal of General Physiology

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ABST R ACT The in vivo peak emission wavelengths of bioluminescence are reported for 15 species of American fireflies. A spectrophotometric study of the dorsal light organs of 155 specimens of the Jamaican firefly Pyrophorus plagiophthalamus showed three distinct color distributions with peak emission wavelengths at 550.1 4-1.5 mu, 556.8 4-1.4 m/z, and 562.4 4-1.0 m/z. Similar spectral measurements of 35 ventral light organs of the same insects gave peak emission wavelengths ranging from 547 through 594 m/z. This is a wider distribution than the total range of all 34 species of firefly studied to date. There was no obvious correlation between the colors of the ventral and dorsal light organs. It appears that P. plagiophthalamus is a special case in which the luciferase enzyme is not only different among members of the same species, but it may be different for the dorsal and ventral light organs in a single individual, A minimum of six different luciferase molecules for P. plagiophthalamus ventral light organs is proposed. The statistical precision in making these spectrophotometric measurements is discussed. I N T R O D U C T I O NIn a previous paper (1) a s u m m a r y through 1963 of all measurements of the in vivo bioluminescence emission spectra of fireflies was presented. This included 20 species, both American and J a m a i c a n , measured by photoelectric spectrometry (2, 3). T h e present paper extends the d a t a to include an additional 15 American species. In addition we have completed an extensive study of the emission spectra of 301 specimens of the J a m a i c a n firefly, Pyrophorus plagiophthalamus, a species which exhibits an unusual intraspecies variability in the color of light emitted. F r o m a statistical analysis of these data, it might be possible to dcduce that there exist structural differences in the "luciferasc" enzyme molecules responsible for light emission in the firefly.

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Section: Plagiophthalamusmentioning

confidence: 91%

The Spectral Distribution of Firefly Light. II

Biggley

Lloyd

Seliger

1967

The Journal of General Physiology

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“…The typical emission spectrum for luciferase is in the yellow-green region (550-570 nm), with a peak at 562 nm at basic media (pH $ 7.5-7.8) (9). However, luciferase is a pH-sensitive enzyme, and acid media (pH $ 5-6) can shift the emission to red (maximum at 620 nm), as well as higher temperatures and heavy metal cations (10).…”

Section: Firefly Luciferasementioning

confidence: 99%

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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“…Insect luciferase is an unusual enzyme produced by the Jamaican click beetle (Pyrophorus plagiophthalamus) (25) or the North American firefly (Photinuspyralis) (18), for instance. The enzyme uses D-luciferin, 02, and ATP as substrates and produces AMP, oxyluciferin, PPi, water, and light (547 to 617 nm) as end products (3).…”

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Nitric oxide donor-mediated killing of bioluminescent Escherichia coli

Virta

Karp

Vuorinen

1994

Antimicrob Agents Chemother

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The antimicrobial activities of two nitric oxide-releasing compounds against Escherichia coli were investigated by using recombinant E. coli cloned with a luciferase gene from Pyrophorus plagiophthalamus. Since luciferase uses intracellular ATP to generate visible light which can be measured from living cells in real time, we wanted to compare-the extent to which cell viability parallels light emission. Results from luminescence measurements and CFU counts were in good agreement, and the decrease in light emission was shown to provide a rapid and more sensitive indication of cytotoxicity.

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The Spectral Distribution of Firefly Light

Cited by 103 publications

References 2 publications

The Spectral Distribution of Firefly Light. II

The Spectral Distribution of Firefly Light. II

Firefly bioluminescence: A mechanistic approach of luciferase catalyzed reactions

Nitric oxide donor-mediated killing of bioluminescent Escherichia coli

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