Firefly Chemiluminescence and Bioluminescence: Efficient Generation of Excited States

Abstract

Firefly luciferase catalyzes a light-emitting reaction in which an excited-state product is formed. Both experimental and theoretical methodologies are used to study this system, and the reactions catalyzed by luciferase are relatively well characterized. However, the mechanism by which an excited-state product is formed is still unknown. This Minireview deals with the current understanding of firefly bioluminescence and chemiluminescence. Thermal decomposition of simple 1,2-dioxetanes is also discussed, due to their role in formation of the excited-state bioluminophore.

A Luciferase Reporter Gene System for High-Throughput Screening of γ-Globin Gene Activators

“…We used a non-lysis substrate system (no detergent) to test the HTS hits, and then compare the activity with the lysis substrate (Steady-Glo) activity to identify potential false positives. Our rationale is that firefly luciferase binders stabilize the enzyme and increase the protein concentration [1][2][3][4][5][6]. In the Steady-Glo ® substrate system, the strong detergent used to lyse cells would dissociate the inhibitor and the enzyme, resulting in higher activity.…”

“…Firefly luciferase has been engineered to be stable and have robust activity [4]. Its activity requires luciferin, ATP, and Mg 2+ [5]. Renilla luciferase catalyzes the oxidative decarboxylation of coelenterazine in the presence of dissolved oxygen to produce blue light [6][7][8].…”

Implication of Arg213 and Arg337 on the kinetic and structural stability of firefly luciferase

“…Firefly luciferase catalyzes the oxidation of luciferin in presence of ATP, Mg 2+ and molecular oxygen to produce photon in the visible range ( max = 560) with high quantum yield [1][2][3][4]. Among various species of firefly luciferases that have been sequenced and crystal structure of them determined [5][6][7][8][9], majority of the studies have been done on Photinus pyralis luciferase; which is a single polypeptide chain, containing 550 amino acids.…”

Effect of very high magnetic field on the optical properties of firefly light emitter oxyluciferin

“…Iwasaka and his co-workers demonstrated, using living fireflies, that firefly bioluminescence was suppressed in intensity and red-shifted for $10 nm when exposed to a 14 T magnetic field. As an ideal "cold light" system with extremely high quantum yield of up to 41.077.4% [5], firefly bioluminescence lies in the center of biochemistry research [6][7][8][9][10][11][12][13][14][15][16][17][18][19]. The revealing of magnetic field effects on firefly bioluminescence therefore represents significant progress in this field.…”