Quantum efficiency of <i>Cypridina</i> luminescence, with a note on that of <i>Aequorea</i>

Johnson, Frank H.; Shimomura, Osamu; Saiga, Yo; Gershman, Lewis C.; Reynolds, George T.; Waters, J. R.

doi:10.1002/jcp.1030600111

Cited by 200 publications

(92 citation statements)

References 22 publications

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“…Green fluorescent protein, GFP, is a spontaneously fluorescent protein composed of ~238 amino acids (~ 27 kDa as a monomer) that absorbs blue light and re-emits it as green fluorescence [1,2]. The fluorescent chromophore originates from an internal Ser-Tyr-Gly sequence that is post-translationally modified in the presence of molecular oxygen to form a fluorescent ring structure that is maximally excited at either 395 nm or 475 nm and emits at 505-515 nm [1,2,3].…”

Section: Introductionmentioning

confidence: 99%

“…The fluorescent chromophore originates from an internal Ser-Tyr-Gly sequence that is post-translationally modified in the presence of molecular oxygen to form a fluorescent ring structure that is maximally excited at either 395 nm or 475 nm and emits at 505-515 nm [1,2,3]. GFP from the hydromedusa Aequorea victoria has been sequenced and is now widely used as a reporter gene for transcriptional studies at the molecular level while mutants from A. victoria and other cnidarians with different fluorescent emission properties from blue to red have also been described [3].…”

Section: Introductionmentioning

confidence: 99%

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Quenching of superoxide radicals by green fluorescent protein

Bou-Abdallah

Chasteen

Lesser

2006

Biochimica et Biophysica Acta (BBA) - General Subjects

161

144

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Green fluorescent protein (GFP) is a widely used in vivo molecular marker. These proteins are particularly resistant, and maintain function, under a variety of cellular conditions such as pH extremes and elevated temperatures. Green fluorescent proteins are also abundant in several groups of marine invertebrates including reef-forming corals. While molecular oxygen is required for the post-translational maturation of the protein, mature GFPs are found in corals where hyperoxia and reactive oxygen species (ROS) occur due to the photosynthetic activity of algal symbionts. In vitro spin trapping electron paramagnetic resonance and spectrophotometric assays of superoxide dismutase (SOD)-like enzyme activity show that wild type GFP from the hydromedusa, Aequorea victoria, quenches superoxide radicals (O 2 •− ) and exhibits SOD-like activity by competing with cytochrome c for reaction with O 2 •− . When exposed to high amounts of O 2 •− the SOD-like activity and protein structure of GFP are altered without significant changes to the fluorescent properties of the protein. Because of the distribution of fluorescent proteins in both the epithelial and gastrodermal cells of reef-forming corals we propose that GFP, and possibly other fluorescent proteins, can provide supplementary antioxidant protection.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Quenching of superoxide radicals by green fluorescent protein

Bou-Abdallah

Chasteen

Lesser

2006

Biochimica et Biophysica Acta (BBA) - General Subjects

161

144

View full text Add to dashboard Cite

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“…The characteristic greenish bioluminescence of the jellyfish, Aequorea victoria, clearly visible as a ring of bright light along the margin of the umbrella [1], is due to the action of two closely associated proteins: aequorin, a small Ca2÷-binding protein (21.4 kDa) [2~1], and a green fluorescent protein (GFP, 27 kDa, fluorescence 2max = 508 nm) [5][6][7][8][9]. The latter contains a chromophore that is the ultimate emitter in the bioluminescence reaction [8,10].…”

Section: Introductionmentioning

confidence: 99%

“…If the reaction is carried out in the presence of excess GFP, a greenish luminescence is observed, identical to that seen in the living animal. The greenish luminescence results from an energy transfer from the excited state of BFP to GFP [6,11,12].…”

Section: Introductionmentioning

confidence: 99%

Evidence for redox forms of the Aequorea green fluorescent protein

1994

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Highly purified recombinant Aequorea green fluorescent protein is able to undergo a reversible oxidation-reduction reaction in the presence of molecular oxygen. In the oxidized form in near UV light, the protein is highly fluorescent, but when reduced with sodium dithionite, it becomes completely non-fluorescent. On exposure to molecular oxygen the reduced, non-fluorescent protein reverts to its original fluorescent state.

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“…The blue fluorescent protein is made up of coelenteramide bound to apoaequorin and the excited state coelenteramide is the emitter in the reaction. If GFP is added to the reaction mixture, however, a bluish-green light (&,, = 508 nm), identical to that of the in vivo luminescence of the animal, is observed due to a radiationless energy transfer from the blue fluorescent protein to GFP [5,6,11]. The green light emission may be schematically outlined, as follows: The genes for apoaequorin and GFP have been cloned and the primary structure of the proteins deduced from the nucleotide sequence [3,12].…”

Section: Introductionmentioning

confidence: 99%

Aequorea green fluorescent protein

1994

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Expression of the cDNA for Aequorea green fluorescent protein in E. coli yielded a fused protein with fluorescence excitation and emission spectra virtually identical to those of the native green fluorescent protein. Further, a solution of the protein, when mixed with aequorin and calcium ion, emitted a greenish luminescence characteristic of the in vivo luminescence of the animal, indicating a radiationless energy transfer to the protein.

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Quantum efficiency of Cypridina luminescence, with a note on that of Aequorea

Cited by 200 publications

References 22 publications

Quenching of superoxide radicals by green fluorescent protein

Quenching of superoxide radicals by green fluorescent protein

Evidence for redox forms of the Aequorea green fluorescent protein

Aequorea green fluorescent protein

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