J Woodland Hastings, Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts, USA
Kurt L Krause, Department of Biology and Biochemistry, University of Houston, Houston, Texas, USA
Published online: January 2006
DOI: 10.1038/npg.els.0003064
Luciferases are enzymes that catalyse reactions in living organisms that result in light emission. There are many different luciferases, different in the sense that the genes and proteins involved are unrelated in evolution, and evidently originated and evolved independently.
Keywords: luciferase proteins; bioluminescence; chemiluminescence; antenna proteins; green fluorescent protein; yellow fluorescent protein
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Figure 1. Bacterial luciferase reaction scheme.
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Figure 2. Organization of bacterial lux genes.
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Figure 3. Ribbon diagram of luciferase from V. harveyi. The chain is shown in red (above), while the chain is shown in green (below). As can be seen the C-termini of the strands comprising the core of the / barrels in each chain face in opposite directions. The four helices in centre of the figure comprise the helix–bundle interaction at the heterodimer interface.
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Figure 4. Schematic of scintillons.
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Figure 5. Lingulodinium polyedrum luciferase (137 kDa).
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Figure 6. Ribbon diagram of the structure of domain 3 of luciferase from Lingulodinium polyedra. Helices are shown in red, strands in yellow and coils in green. The central 10-stranded -barrel is shown flanked on either side by helical and coil structures. At the top of the figure, the N-terminal domain is shown at left next to the helix-turn-helix motif that proceeds directly out of the 10-stranded barrel.
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Figure 7. Coelenterate luciferase reaction intermediates.
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Figure 8. Ribbon diagram of the photoprotein obelin from the colonial hydroid, Obelia sp. The coelenterazine–oxygen adduct is shown in green buried in the interior of the cluster of blue E-F hand motifs that make up the aequorin structure. The eight helices pack together in a topology that has been depicted as two cups stacked ‘rim to rim’.
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Figure 9. GFP chromophore.
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Figure 10. Ribbon diagram of green fluorescent protein shown illustrating its unique -can topology. Inside of the -can the three residues (modified from Ser65, Tyr66 and Gly67) that form the emitter are shown in blue.
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Figure 11. Ribbon diagram of firefly luciferase. The large N-terminal domain is below and to the left with the small C-terminal domain above and to the right. The large cleft between these two domains is readily visible. Locations of the two bromoform molecules are shown in blue and red. The blue bromoform molecule is located at the proposed luciferin binding site.
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| References | |
| Conti WR, Franks NP and Brick P (1996) Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure 4: 287–298. | |
| Fisher AJ, Raushel FM, Baldwin TO and Rayment L (1995) Three-dimensional structure of bacterial luciferase from Vibrio harveyi at 2.4 Å resolution. Biochemistry 34: 6581–6586. | |
| Fisher AJ, Thompson TB, Thoden JB, Baldwin TO and Rayment I (1996) The 1.5-Å resolution crystal structure of bacterial luciferase in low salt conditions. Journal of Biological Chemistry 271: 21956–21968. | |
| Franks NP, Jenkins A, Conti WR and Brick P (1998) Structural basis for the inhibition of firefly luciferase by a general anesthetic. Biophysical Journal 75: 2205–2211. | |
| Head JF, Inouye K, Teranishi O and Shimomura (2000) The crystal structure of photoprotein Aequorin at 2.3 Å resolution. Nature 405: 372–376. | |
| Liu ZJ, Vysotski ES, Chen CJ et al. (2000) Structure of the Ca2+-regulated photoprotein obelin at 1.7. A resolution determined directly from its sulfur substructure. Protein Science 9: 2085–2093. | |
| Ormö M, Cubitt AB, Kallio K et al. (1996) Crystal structure of the Aequorea victoria green fluorescent protein. Science 273: 1392–1395. | |
| Schultz W, Liu L, Cegielski M and Hastings JW (2005) Structure and mechanism of pH regulation in a luciferase from the marine dinoflagellate Lingulodinium polyedrum. Proceedings of the National Academy of Sciences of the USA 102: 1378–1383. | |
| Tanner JJ, Miller MD, Wilson KS, Tu SC and Krause KL (1997) Structure of bacterial luciferase beta 2 homodimer: implications for flavin binding. Biochemistry 36: 665–672. | |
| Yang F, Moss LG and Phillips GN Jr. (1996) The molecular structure of green fluorescent protein. Nature Biotechnology 14: 1246–1251. | |
| Further Reading | |
| Blinks JR, Wier WG, Hess P and Prendergast FG (1982) Measurement of Ca+ concentrations in living cells. Progression in Biophysics and Molecular Biology 40: 1–114. | |
| Buck JB and Buck E (1976) Synchronous fireflies. Scientific American 234: 74–85. | |
| book Chalfie M and Kain S (eds) (2005) Green Fluorescent Protein Second Edition. New York: Wiley. | |
| book DeLuca M and McElroy WD (eds) (1986) "Bioluminescence and chemiluminescence". Methods in Enzymology, vol. 133, p. 649. New York: Academic Press. | |
| book Harvey EN (1952) Bioluminescence, p. 649. New York: Academic Press. | |
| Hastings JW (1983) Biological diversity, chemical mechanisms and evolutionary origins of bioluminescent systems. Journal of Molecular Evolution, 19: 309–321. | |
| book Hastings JW and Morin JG (1991) "Bioluminescence". In: Prosser CL (ed.) Neural and Integrative Animal Physiology, pp. 131–170. New York: Wiley | |
| Hastings JW, Potrikus CJ, Gupta S, Kurfürst M and Makemson JC (1985) Biochemistry and physiology of bioluminescent bacteria. Advances in Microbial Physiology 26: 235–291. | |
| book Herring PJ (ed.) (1978) Bioluminescence in Action, p. 570. New York: Academic Press. | |
| Meighen EA and Dunlap PV (1993) Physiological, biochemical and genetic control of bacterial bioluminescence. Advances in Microbial Physiology 34: 1–67. | |
| Wilson T and Hastings JW (1998) Bioluminescence. Annual Review Cell and Developmental Biology 14: 197–230. | |
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