@article {23166,
	title = {The origin, diversity, and structure function relationships of insect luciferases},
	journal = {CMLS Cellular and Molecular Life Sciences},
	volume = {59},
	number = {11},
	year = {2002},
	note = {Literature-Review; ArticleEnglish},
	pages = {1833-1850},
	abstract = {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 acylCoA 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.},
	keywords = {121295-11-2Q; 9013-18-7; 9014-00-0Q; 61869-41-8Q; 61969-99-1Q; 61970-00-1Q; 62213-54-1Q; 76106-81-5Q; 2591-17-5Q; 7273-34-9Q; 21730-91-6Q; 50909-86-9Q; 55779-48-1Q; 58947-91-4Q; 61369-27-5Q; 121295-11-2Q; light-emission, 21730-91-6Q, 50909-86-9Q, 55779-48-1Q, 58947-91-4Q, 61369-27-5Q, 61869-41-8Q, 61969-99-1Q, 61970-00-1Q, 62213-54-1Q, 7273-34-9Q, 76106-81-5Q; luciferin-: 2591-17-5Q, Animalia-; beetle- (Coleoptera-): common-; Coleoptera-: Animals-, Arthropoda-, Arthropods-, Enzymology-: Biochemistry-and-Molecular-Biophysics; [75304-] Coleoptera-, Insecta-, Insects-, Invertebrata-, Invertebrates-; firefly-; acyl-CoA: acyl-coenzyme-A; acyl-CoA-ligases: 9013-18-7; luciferases-: 9014-00-0Q},
	url = {http://www.online-keys.net/sciaroidea/add01/Viviani_2002_Luciferace.pdf},
	author = {Viviani, Vadim R.}
}
@article {23167,
	title = {Two bioluminescent diptera: The North American Orfelia fultoni and the Australian Arachnocampa flava. Similar niche, different bioluminescence systems},
	journal = {Photochemistry and Photobiology},
	volume = {75},
	number = {1},
	year = {2002},
	note = {ArticleEnglish},
	pages = {22-27},
	abstract = {Orfelia fultoni is the only bioluminescent dipteran (Mycetophilidae) found in North America. Its larvae live on stream banks in the Appalachian Mountains. Like their Australasian relative Arachnocampa spp., they build sticky webs to which their bioluminescence attracts flying prey. They bear two translucent lanterns at the extremities of the body, histologically distinct from the single caudal lantern of Arachnocampa spp., and emit the bluest bioluminescence recorded for luminescent insects (lambdamax=460 nm versus 484 nm from Arachnocampa). A preliminary characterization of these two bioluminescent systems indicates that they are markedly different. In Orfelia a luciferin-luciferase reaction was demonstrated by mixing a hot extract prepared with dithiothreitol (DTT) under argon with a crude cold extract. Bioluminescence is not activated by adenosine triphosphate (ATP) but is strongly stimulated by DTT and ascorbic acid. Using gel filtration, we isolated a luciferase fraction of apprx140 kDa and an additional high molecular weight fraction (possibly a luciferin-binding protein) that activated bioluminescence in the presence of luciferase and DTT. The Arachnocampa luciferin-luciferase system involves a 36 kDa luciferase and a luciferin soluble in ethyl acetate under acidic conditions; the bioluminescence is activated by ATP but not by DTT. The present findings indicate that the bioluminescence of O. fultoni constitutes a novel bioluminescent system unrelated to that of Arachnocampa.},
	keywords = {111839-44-2Q; argon-: 7440-37-1; ascorbic-acid: 50-81-7Q, 121295-11-2Q; Appalachian-Mountains: USA-, 21730-91-6Q, 42530-29-0Q, 50909-86-9Q, 55779-48-1Q, 58947-91-4Q, 61369-27-5Q, 61869-41-8Q, 61969-99-1Q, 61970-00-1Q, 62213-54-1Q, 62624-30-0Q; dithiothereitol-: DTT-; ethyl-acetate: 141-78-6; luciferase-: 9014-00-0Q, 7273-34-9Q, 76106-81-5Q; luciferin-: 2591-17-5Q, 94587-45-8Q, Animalia-; Arachnocampa-flava (Diptera-): Australian-, Arthropoda-, Arthropods-, Bioenergetics-: Biochemistry-and-Molecular-Biophysics; Radiation-Biology; [75314-] Diptera-, bioluminescent-, bioluminescent-; Keroplatus- (Diptera-): bioluminescent-; Orfelia-fultoni (Diptera-): North-American, Insecta-, Insects-, Invertebrata-, Invertebrates-; caudal-lantern; ATP-: 56-65-5Q, larvae-; Diptera-: Animals-, Nearctic-region; 56-65-5Q; 42530-29-0Q; 94587-45-8Q; 111839-44-2Q; 7440-37-1; 50-81-7Q; 62624-30-0Q; 141-78-6; 9014-00-0Q; 61869-41-8Q; 61969-99-1Q; 61970-00-1Q; 62213-54-1Q; 76106-81-5Q; 2591-17-5Q;, North-America},
	url = {http://www.online-keys.net/sciaroidea/add01/Viviani_et_al_2002_fultoni_\&_aracnocampa.pdf},
	author = {Viviani, Vadim R. and Hastings, J. Woodland and Wilson, Therese}
}
