John Lee

Department of Biochemistry and Molecular Biology
University of Georgia, Athens, GA 30602

These two books by E. Newton Harvey provide a comprehensive account of the developments in this field of study, from antiquity to the mid-twentieth century.

A History of Luminescence. From the Earliest Times Until 1900.
The American Philosophical Society, Philadelphia, 692 pp. (1957).

Bioluminescence. Academic Press, New York, 640 pp. (1952).

The significant advances, in recent times, from studies of the biochemical aspects of bioluminescence, are listed below according to the year of publication.

The energy source for bioluminescence in an isolated system.
W.D. McElroy. Proc. Natl. Acad. Sci. USA 33: 342-345.
Adenosine triphosphate (ATP) is an essential requirement for the in vitro reaction of firefly bioluminescence.

The requirement of riboflavin phosphate for bacterial luminescence.
W.D.McElroy, J.W. Hastings, V. Sonnefeld, and J. Coulombre. Science 118: 385-386.
Reduced flavin mononucleotide (FMNH2) is one essential requirement being reduced by NADH.

Isolation, identification, and function of long chain fatty aldehydes affecting the bacterial luciferin-luciferase reaction.
B.L. Strehler and M.J. Cormier. J. Biol. Chem. 211: 213-225.

Determination of ATP and related compounds.
Firefly luminescence and other methods.
B.L. Strehler and J.R. Totter. Methods Biochem. Anal. 1; 341-356.
The first suggestion of the firefly protocol, which did not come into full realization until 1967.

Crystalline firefly luciferase.
A.A. Green and W.D. McElroy. Biochim. Biophys Acta 20: 170-176.
Firefly luciferase was purified as a protein with a mass around 100 kDa.

Quantum yield of the oxidation of firefly luciferin.
H. H. Seliger and W.D. McElroy. Biochem. Biophys. Res. Commun. 1: 21-24.
The efficiency was measured to be near unity.

The structure and synthesis of firefly luciferin.
E.H. White, F. McCapra, G. Field, and W.D. McElroy.
J. Amer. Chem. Soc. 85: 337-343.

Extraction, purification and properties of aequorin, a bioluminescent protein from the hydromedusan, Aequorea.
O. Shimomura, F.H. Johnson, and Y. Saiga.
J. Cell. Comp.. Physiol. 59: 223-239.
Aequorin was named a "photoprotein", as it required only Ca2+ and not oxygen for light emission.

Intermediates in the bioluminescent oxidation of reduced flavin mononucleotide.
J.W. Hastings and Q.H. Gibson. J. Biol. Chem. 238: 2537-2554.
A stopped-flow study revealed a long-lived intermediate, probably a flavin-peroxide.

Absolute spectral sensitivity of phototubes, and the application to the measurement of the absolute quantum yield of chemiluminescence and bioluminescence.
J. Lee and H.H. Seliger. Photochem. Photobiol. 4: 1015-1048.

Cypridina bioluminescence. Structure of Cypridina luciferin.
Y. Kishi, T. Goto, Y. Hirata, O. Shimomura, and F. H. Johnson.
Tetrahedron Lett. No. 29, 3427-3436.

Determination of picogram amounts of ATP using the luciferin-luciferase enzyme system.
G.E. Lyman and J.P. DeVincenzo. Anal. Biochem. 21; 435-443.

The chemiluminescence of a Cypridina luciferin analog.
F. McCapra and Y. Chang. Chem. Commun. 1011-1012.
A foundation for the mechanism of many marine bioluminescence reactions.

The characterization of scintillons, bioluminescent particles from the marine dinoflagellate, Gonyaulax polyhedra.
R. DeSa and J.W. Hastings. J. Gen. Physiol. 51: 105-123.

Structurally distinct bacterial luciferases.
J.W. Hastings, K. Weber, J. Friedland, A. Eberhard, G.W. Mitchell, and A. Gunsalus. Biochemistry 8: 4681-4689.
Bacterial luciferase is a heterodimer with each subunit mass around 40 kDa.

Chemi- and bioluminescence of firefly luciferin.
E.H. White, E. Rapaport, T.A. Hopkins, and H.H. Seliger. J. Amer. Chem. Soc. 91; 2178-2180.
A red shifted bioluminescence induced by pH attributed to keto-enol tautomerism in the excited state.

From 1970 on, there was a great deal of research output in the field, making the choice of key papers quite arguable. These following four are cited as particularly significant.

The cellular control of the synthesis and activity of the bacterial luminescent system.
Nealson, K., Platt, T., and Hastings, J.W. J. Bact. 104: 313-322.
Among the first studies to recognize that some factor, now recognized as an "autoinducer", functions in cell-cell communication.

Mechanism of luminescent oxidation of Cypridina luciferin.
O. Shimomura and F.H. Johnson. Biochem. Biophys. Res. Commun. 44: 340-346.
A dioxetanone intermediate was proposed from product analysis of the reaction using oxygen-18.

The use of the luminescent bacterial system for the rapid assessment of aquatic toxicity.
A.A. Bulich and D.L. Isenberg. ISA Trans. 20: 29-33.
This technical report was the basis of a patent, which resulted in the widest application of bioluminescence methodology.

Primary structure of the Aequorea victoria green-fluorescent protein.
D.C. Prasher, V.K. Eckenroad, W.W. Ward, and M.J. Cormier.
Gene 111: 229-233.
The result of this cloning, and later expression, of GPF was a revolution in biotechnology applications.


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