Evolution of beetle bioluminescence: the origin of beetle luciferin

Abstract

Bioluminescence, the conversion of chemical energy into light in living organisms, is dependent on two principal components, an enzyme luciferase and the substrate luciferin. In beetles, the enzyme luciferase has been extensively studied, with significant enzymological, sequence and structural data now available. Furthermore, the enzyme has been employed in a remarkable number of important applications, from microbial detection and medical imaging to GM gene expression studies. However, there is little information regarding the biosynthesis of beetle luciferin, and here we review the literature and speculate as to its evolutionary origins. Luciferin consists of a benzothiazole moiety attached to a thiazole carboxylic acid moiety, the former being rarely observed in nature but the latter being observed in a broad range of biologically derived molecules. Benzothiazoles are, however, observed in melanogenesis and we speculate as to whether this may be relevant to the understanding of luciferin biosynthesis in beetles. This review examines recent novel insights into beetle luciferin recycling and we assess a range of possible biosynthetic mechanisms.

Firefly bioluminescence: A mechanistic approach of luciferase catalyzed reactions

“…3; (13-15)], which was proposed and confirmed on the basis of chemical synthesis (13) and X-ray crystallography (16). In Nature, however, the biochemical pathway for LH 2 synthesis remains a mystery (15). In fact it is not even known if the fireflies contain all enzymes to synthesize LH 2 or if it is obtained by ingestion of other bioluminescent organisms or by symbiosis with bacteria (15).…”

“…In Nature, however, the biochemical pathway for LH 2 synthesis remains a mystery (15). In fact it is not even known if the fireflies contain all enzymes to synthesize LH 2 or if it is obtained by ingestion of other bioluminescent organisms or by symbiosis with bacteria (15). Also, the evolutionary creation of LH 2 is questioned.…”

“…Some researchers propose that LH 2 first served as an antioxidant, later being requested by the bioluminescent reaction when luciferase appeared (17). It has been suggested that the origin of the thiazoline ring could be a cysteine (15), as can be observed in the chemical synthesis in which one of the steps involves this amino acid (18). Cysteine has two isomers, L-and D-, and either one of them can be used to form LH 2 , giving rise to L-LH 2 and D-LH 2 , respectively.…”

Theoretical Study of the Relationships between Excited State Geometry Changes and Emission Energies of Oxyluciferin

“…[1][2][3][4] Interestingly, while keto-1 exhibits red fluorescence in DMSO or in aqueous solution, 2,3,[5][6][7][8][9] its bioluminescence spectra can be shifted to the green by interactions with the luciferases. [10][11][12][13][14][15][16] Several mechanisms have been proposed to explain this phenomenon. 1,2,4,6,11,12,14,[17][18][19][20][21][22][23][24][25] To the present, the detailed mechanism of the bioluminescence and its shifts in color remain unclear due to the complexity of the microenvironment in vivo.…”

Les calmars des grands fonds attaquent avec des « tentacules de lumière »

“…Pour produire de la lumière, chaque groupe d'organismes a, au cours de son évolution, indépen-damment « inventé » son enzyme pour produire de la lumière. Étonnamment, il n'existe aucune conservation protéique entre ces différentes luciférases [3]. Plusieurs séquences de ces enzymes sont désormais utilisées in vivo et in vitro comme « gène rapporteur ».…”