NDLI: Interaction of firefly luciferase with substrates and their analogs: a study using fluorescence spectroscopy methods

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Photochemical & Photobiological Sciences Vol -6

Photochemical & Photobiological Sciences Vol -5

Photochemical & Photobiological Sciences Vol -4

Photochemical & Photobiological Sciences Vol -3

Photochemical & Photobiological Sciences Vol -2

Interaction of firefly luciferase with substrates and their analogs: a study using fluorescence spectroscopy methods

Content Provider	Royal Society of Chemistry (RSC)
Author	Ugarova, Natalia N.
Copyright Year	2008
Abstract	The results of the author's laboratory on the interaction of Luciola mingrelica firefly luciferase with substrates and their analogs using both steady-state and time resolved fluorescence are reviewed. The contribution of fluorescence of Trp and Tyr residues of the protein to its intrinsic fluorescence spectrum was estimated. Studies of quenching of Trp and Tyr fluorescence by luciferin and ATP allowed one to determine binding constants of the luciferase with substrates and to show that the binding of one substrate to the luciferase decreases the affinity of the enzyme for the other one. Fluorescence of oxyluciferin and its analogs (dimethyl- and monomethyloxyluciferins) was shown to be a good model of native firefly bioluminescence. A comparison of the fluorescence spectra of oxyluciferin and its analogs in aqueous solutions and in the presence of the luciferase revealed specific and nonspecific effects of the microenvironment on the equilibrium between different ionic forms of oxyluciferin. An approach based on photo-physical concepts of the correlation between luminescence spectra and structure of the emitter and its microenvironment was proposed and this approach was used to analyze bioluminescence spectra of wild-type and mutant luciferases.
Starting Page	218
Ending Page	227
Page Count	10
File Format	HTM / HTML PDF
ISSN	1474905X
Volume Number	7
Issue Number	2
Journal	Photochemical & Photobiological Sciences
DOI	10.1039/b712895a
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Tyrosine Bioluminescence Enzyme Luciferase Luminescence Fluorescence Firefly Tyr Protein Luciola Trp Luciferin Mutation ATP Adenosine triphosphate
Content Type	Text
Resource Type	Article
Subject	Physical and Theoretical Chemistry

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Quenching of the fluorescence of Tyr and Trp residues of firefly luciferase from Luciola mingrelica by the substrates

Relationship between stability and bioluminescence color of firefly luciferase

Kinetics of inhibition of firefly luciferase by oxyluciferin and dehydroluciferyl-adenylate

The dark and bright sides of an enzyme: a three dimensional structure of the N-terminal domain of Zophobas morio luciferase-like enzyme, inferences on the biological function and origin of oxygenase/luciferase activity

The origin of luciferase activity in Zophobas mealworm AMP/CoA-ligase (protoluciferase): luciferin stereoselectivity as a switch for the oxygenase activity

α-Synuclein enhances bioluminescent activity of firefly luciferase by facilitating luciferin localization

Practical application of bioluminescence enzyme immunoassay using enhancer for firefly luciferin-luciferase bioluminescence.

Dimethyl-and monomethyloxyluciferins as analogs of the product of the bioluminescence reaction catalyzed by firefly luciferase

Bioluminescence Spectra of Native and Mutant Firefly Luciferases as a Function of pH

Interaction of firefly luciferase with substrates and their analogs: a study using fluorescence spectroscopy methods

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Quenching of the fluorescence of Tyr and Trp residues of firefly luciferase from Luciola mingrelica by the substrates

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Interaction of firefly luciferase with substrates and their analogs: a study using fluorescence spectroscopy methods