Excited-state proton transfer and the mechanism of action of firefly luciferase

Bowie, Lemuel J.; Irwin, R. M.; Loken, Michael R.; DeLuca, Marlene; Brand, Ludwig

doi:10.1021/bi00734a002

Cited by 28 publications

(15 citation statements)

References 22 publications

(11 reference statements)

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“…Recently, the cDNA for an enzyme which recycles luciferin from oxyluciferin in the light organ of fireflies was cloned and sequenced, but no similarity was found with other enzymes [66]. Luciferin, dehydroluciferin, and oxyluciferin display similar spectroscopic properties [65,67]. In aqueous media, when the 6¢phenolate proton in the excited state is allowed to dissociate, all display intense yellow-green fluorescence (l max = 530 -540 nm); however, in non-polar solvents, where proton dissociation is not favored, the fluorescence is blue (l max = 430-450 nm) [66].…”

Section: Substrates and Products Of The Firefly Luciferase Reactionmentioning

confidence: 99%

The origin, diversity, and structure function relationships of insect luciferases

Viviani

2002

CMLS, Cell. Mol. Life Sci.

291

295

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Luciferases are the enzymes that catalyze the reactions that produce light in bioluminescence. Whereas the oxidative mechanism which leads to light emission is similar for most luciferases, these enzymes and their substrates are evolutionarily unrelated. Among all bioluminescent groups, insects constitute one of the most diverse in terms of biochemistry. In the fungus-gnats (Mycetophilidae: Diptera), for example, bioluminescence is generated by two biochemically distinct systems. Despite the diversity, investigations on insect luciferases and biochemistry have been conducted mostly with fireflies. The luciferases from the related phengodid beetles, which can produce green to red bioluminescence using the same chemistry as firefly luciferases, have been recently investigated. Beetle luciferases originated from ancestral acyl-CoA ligases. Present data suggest that conserved motifs among this class of ligases are involved in substrate adenylation. The three-dimensional structure of firefly luciferase was recently solved and mutagenesis studies have been performed identifying putative residues involved in luciferin binding and bioluminescence color determination in several beetle luciferases. The knowledge gained through these studies is helping in the development of useful reporter gene tools for biotechnological and biomedical purposes.

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Section: Substrates and Products Of The Firefly Luciferase Reactionmentioning

confidence: 99%

The origin, diversity, and structure function relationships of insect luciferases

Viviani

2002

CMLS, Cell. Mol. Life Sci.

291

295

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“…(ii) Cyclic AMP or cyclic AMP-dependent phosphorylation might also affect the photochemical reaction directly. Thus, Bowie et al (26) have noted that cyclic AMP is the only nucleotide which mimicks ATP-Mg2+ in altering the emission spectrum of a fluorescent active-site probe bound to firefly luciferase. (ATP-Mg24 normally reacts to form the excited enzyme-luciferyladenylate complex necessary for light emission,) This observation raises the possibility that cyclic AMP, generated through neural excitation, could play a regulatory role in photocyte light emission reactions (27).…”

Section: Additionmentioning

confidence: 99%

Octopamine Receptors, Adenosine 3′,5′-Monophosphate, and Neural Control of Firefly Flashing

Nathanson

1979

Science

141

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An adenylate cyclase activated as much as 25-fold by low concentrations of octopamine has been identified in the firefly lantern. The relative potency of octopamine and various other amines in stimulating this enzyme, and effects of antagonists in blocking octopamine activation, correlate well with the known effects of these agents in affecting light production. In addition to suggesting a role for adenosine 3',5'-monophosphate (or pyrophosphate) in the neural control of firefly flashing, identification of this potent enzyme should facilitate the characterization of phenylethylamine receptors in excitable tissue.

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“…The substrate molecule reacted upon, which emits light in such a reaction, is called a luciferin. Luciferases are a wide range of enzymes that catalyse the oxidation of substrate luciferins to yield non-reactive oxyluciferins and the release of photons of light (17)(18)(19)(20)(21). As luciferin substrates are used, they must be replenished, which usually occurs through diet.…”

Section: Luciferin±luciferase±protein Light-emitting Systemsmentioning

confidence: 99%

Imaging of light emission from the expression of luciferases in living cells and organisms: a review

2002

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Luciferases are enzymes that emit light in the presence of oxygen and a substrate (luciferin) and which have been used for real-time, low-light imaging of gene expression in cell cultures, individual cells, whole organisms, and transgenic organisms. Such luciferin-luciferase systems include, among others, the bacterial lux genes of terrestrial Photorhabdus luminescens and marine Vibrio harveyi bacteria, as well as eukaryotic luciferase luc and ruc genes from firefly species (Photinus) and the sea panzy (Renilla reniformis), respectively. In various vectors and in fusion constructs with other gene products such as green fluorescence protein (GFP; from the jellyfish Aequorea), luciferases have served as reporters in a number of promoter search and targeted gene expression experiments over the last two decades. Luciferase imaging has also been used to trace bacterial and viral infection in vivo and to visualize the proliferation of tumour cells in animal models.

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Excited-state proton transfer and the mechanism of action of firefly luciferase

Abstract: The term "hydrophobicity" as used in this paper refers to the sum total of all such environmental effects on fluorescence. For a more complete discussion on hydrophobicity and solvent polarity the reader is referred to the recent review of Brand and Gohlke (1972).

Cited by 28 publications

References 22 publications

The origin, diversity, and structure function relationships of insect luciferases

The origin, diversity, and structure function relationships of insect luciferases

Octopamine Receptors, Adenosine 3′,5′-Monophosphate, and Neural Control of Firefly Flashing

Imaging of light emission from the expression of luciferases in living cells and organisms: a review

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