Coelenterazine

Coelenterazine is a luciferin, a molecule that emits light after reaction with oxygen, found in many aquatic organisms across eight phyla.[1] It is the substrate of many luciferases such as Renilla reniformis luciferase (Rluc), Gaussia luciferase (Gluc), and photoproteins, including aequorin, and obelin. All these proteins catalyze the oxidation of this substance, a reaction catalogued EC 1.13.12.5.

Coelenterazine
Names
IUPAC name
6-(4-Hydroxyphenyl)-2-[(4-hydroxyphenyl)methyl]-8-(phenylmethyl)-7H-imidazo[1,2-a]pyrazin-3-one
Other names
Renilla luciferin
Identifiers
3D model (JSmol)
ChEBI
ChemSpider
ECHA InfoCard 100.164.960
UNII
  • InChI=1S/C26H21N3O3/c30-20-10-6-18(7-11-20)15-23-26(32)29-16-24(19-8-12-21(31)13-9-19)27-22(25(29)28-23)14-17-4-2-1-3-5-17/h1-13,16,27,30-31H,14-15H2 checkY
    Key: YHIPILPTUVMWQT-UHFFFAOYSA-N checkY
  • InChI=1S/C26H21N3O3/c30-20-10-6-18(7-11-20)15-23-26(32)29-16-24(19-8-12-21(31)13-9-19)27-22(25(29)28-23)14-17-4-2-1-3-5-17/h1-13,16,27,30-31H,14-15H2
  • C1=CC=C(C=C1)CC2=C3N=C(C(=O)N3C=C(N2)C4=CC=C(C=C4)O)CC5=CC=C(C=C5)O
Properties
C26H21N3O3
Molar mass 423.472 g·mol−1
Appearance Orange-yellow crystals
Melting point 175 to 178 °C (347 to 352 °F; 448 to 451 K)
Absorbance ε435 = 9800 M−1 cm−1 (methanol)[1]
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
☒N verify (what is checkY☒N ?)
Infobox references

History

Coelenterazine was simultaneously isolated and characterized by two groups studying the luminescent organisms sea pansy (Renilla reniformis) and the cnidarian Aequorea victoria, respectively.[2][3] Both groups independently discovered that the same compound was used in both luminescent systems. The molecule was named after the now-obsolete phylum coelenterata. Likewise, the two main metabolites – coelenteramide and coelenteramine – were named after their respective functional groups. While coelenterazine was first discovered in Aequorea victoria, it was later shown that they do not synthesize coelenterazine, but obtain it through their diet, largely from crustaceans and copepods.[4]

Occurrence

Coelenterazine is widely found in marine organisms including:

The compound has also been isolated from organisms that are not luminescent, such as the Atlantic herring and several shrimp species including Pandalus borealis and Pandalus platyuros.

Biosynthesis

Biosynthesis of coelenterazine in Metridia starts from two molecules of tyrosine and one molecule of phenylalanine, and some researchers believe this comes in the form of a cyclized "Phe-Tyr-Tyr" (FYY) peptide.[6]

Many members of the genus Metridia also produce luciferases that use this compound,[7] some of which are secreted into extracellular space, an unusual property for luciferases.[8]

Properties

Coelenterazine can be crystallized into orange-yellow crystals. The molecule absorbs light in the ultraviolet and visible spectrum, with peak absorption at 435 nm in methanol, giving the molecule a yellow color. The molecule spontaneously oxidizes in aerobic conditions or in some organic solvents such as dimethylformamide and DMSO and is preferentially stored in methanol or with an inert gas.

Synthetic coelenterazine derivatives

To improve its biophysical properties, derivatives of coelenterazine have been synthesized by means of different procedures including multicomponent strategies.[9]

See also

References
  1. Shimomura, O. (2006). Bioluminescence: Chemical Principles and Methods. World Scientific Publishing. pp. 159–65. ISBN 978-981-256-801-4.
  2. Hori K, Charbonneau H, Hart RC, Cormier MJ (October 1977). "Structure of native Renilla reinformis luciferin". Proceedings of the National Academy of Sciences of the United States of America. 74 (10): 4285–7. Bibcode:1977PNAS...74.4285H. doi:10.1073/pnas.74.10.4285. PMC 431924. PMID 16592444.
  3. Shimomura O, Johnson FH (April 1975). "Chemical nature of bioluminescence systems in coelenterates". Proceedings of the National Academy of Sciences of the United States of America. 72 (4): 1546–9. Bibcode:1975PNAS...72.1546S. doi:10.1073/pnas.72.4.1546. PMC 432574. PMID 236561.
  4. Haddock SH, Rivers TJ, Robison BH (September 2001). "Can coelenterates make coelenterazine? Dietary requirement for luciferin in cnidarian bioluminescence". Proceedings of the National Academy of Sciences of the United States of America. 98 (20): 11148–51. Bibcode:2001PNAS...9811148H. doi:10.1073/pnas.201329798. PMC 58698. PMID 11572972.
  5. Haddock SHD, Case JF (1994). "A bioluminescent chaetognath" (PDF). Nature. 367 (6460): 225–26. Bibcode:1994Natur.367..225H. doi:10.1038/367225a0. S2CID 4362422. Archived from the original (PDF) on 2008-05-16. Retrieved 2008-10-28.
  6. Francis WR, Shaner NC, Christianson LM, Powers ML, Haddock SH (30 June 2015). "Occurrence of Isopenicillin-N-Synthase Homologs in Bioluminescent Ctenophores and Implications for Coelenterazine Biosynthesis". PLOS ONE. 10 (6): e0128742. Bibcode:2015PLoSO..1028742F. doi:10.1371/journal.pone.0128742. PMC 4488382. PMID 26125183.
  7. Tessler M, Gaffney JP, Crawford JM, Trautman E, Gujarati NA, Alatalo P, et al. (14 September 2018). "Metridia lucens". PeerJ. 6: e5506. doi:10.7717/peerj.5506. PMC 6140675. PMID 30233994.
  8. Markova SV, Golz S, Frank LA, Kalthof B, Vysotski ES (January 2004). "Cloning and expression of cDNA for a luciferase from the marine copepod Metridia longa. A novel secreted bioluminescent reporter enzyme". The Journal of Biological Chemistry. 279 (5): 3212–7. doi:10.1074/jbc.M309639200. PMID 14583604.
  9. Vece V, Vuocolo G (2015). "Multicomponent Synthesis of Novel Coelenterazine Derivatives Substituted at the C-3 Position". Tetrahedron. 71 (46): 8781–85. doi:10.1016/j.tet.2015.09.048.
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