Vargulin

Last updated
Vargulin
Vargulin.svg
Names
IUPAC name
2-[3-[2-[(2S)-butan-2-yl]-6-(1H-indol-3-yl)-3-oxo-7H-imidazo[2, 1-c]pyrazin-8-yl]propyl]guanidine
Other names
Cypridina luciferin, cypridinid luciferin, Vargula luciferin
Identifiers
3D model (JSmol)
ChemSpider
PubChem CID
UNII
  • InChI=1S/C22H27N7O/c1-3-13(2)19-21(30)29-12-18(15-11-26-16-8-5-4-7-14(15)16)27-17(20(29)28-19)9-6-10-25-22(23)24/h4-5,7-8,11-13,26-27H,3,6,9-10H2,1-2H3,(H4,23,24,25) Yes check.svgY
    Key: ZWPWSXGBDMGKKS-UHFFFAOYSA-N Yes check.svgY
  • InChI=1S/C22H27N7O/c1-3-13(2)19-21(30)29-12-18(15-11-26-16-8-5-4-7-14(15)16)27-17(20(29)28-19)9-6-10-25-22(23)24/h4-5,7-8,11-13,26-27H,3,6,9-10H2,1-2H3,(H4,23,24,25)/t13-/m0/s1
    Key: ZWPWSXGBDMGKKS-UHFFFAOYAG
  • O=C\3N4\C=C(\c2c1ccccc1[nH]c2)N/C(=C4/N=C/3[C@@H](C)CC)CCC/N=C(\N)N
Properties
C22H27N7O
Molar mass 405.506 g·mol−1
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
X mark.svgN  verify  (what is  Yes check.svgYX mark.svgN ?)

Vargulin, [1] also called Cypridinid luciferin, [2] Cypridina luciferin, or Vargula luciferin, is the luciferin found in the ostracod Cypridina hilgendorfii , also named Vargula hilgendorfii . [3] These bottom dwelling ostracods emit a light stream into water when disturbed presumably to deter predation. Vargulin is also used by the midshipman fish, Porichthys.

Contents

History

A partial extraction procedure was developed in 1935 which involved reacting the compound with benzoyl chloride to allow it to be separated from the water-soluble components. [4] The compound was first isolated and purified to crystals by Osamu Shimomura. [5] The structure of the compound was confirmed some years later. [6] Feeding experiments suggest that the compound is synthesized in the animal from three amino-acids: tryptophan, isoleucine, and arginine. [7]

Biochemistry

Vargulin is oxidized by the Vargula luciferase, [8] a 62 kDa enzyme, to produce blue light at 462 nm (max emission, detected with a 425 to 525 nm filter). The vargulin does not cross react with luciferases using coelenterazine or Firefly luciferin.

Uses

Vargulin (with the associated luciferase) has applications in biotechnology:

Although less stable, the Cypridina system is useful because can be used in multiplex assays with other (red-emitting) luciferin assays.

Related Research Articles

<span class="mw-page-title-main">Bioluminescence</span> Emission of light by a living organism

Bioluminescence is the production and emission of light by living organisms. It is a form of chemiluminescence. Bioluminescence occurs widely in marine vertebrates and invertebrates, as well as in some fungi, microorganisms including some bioluminescent bacteria, and terrestrial arthropods such as fireflies. In some animals, the light is bacteriogenic, produced by symbiotic bacteria such as those from the genus Vibrio; in others, it is autogenic, produced by the animals themselves.

<span class="mw-page-title-main">Luciferase</span> Enzyme family

Luciferase is a generic term for the class of oxidative enzymes that produce bioluminescence, and is usually distinguished from a photoprotein. The name was first used by Raphaël Dubois who invented the words luciferin and luciferase, for the substrate and enzyme, respectively. Both words are derived from the Latin word lucifer, meaning "lightbearer", which in turn is derived from the Latin words for "light" (lux) and "to bring or carry" (ferre).

<span class="mw-page-title-main">Ostracod</span> Class of crustaceans

Ostracods, or ostracodes, are a class of the Crustacea, sometimes known as seed shrimp. Some 33,000 species have been identified, grouped into 7 valid orders. They are small crustaceans, typically around 1 mm (0.04 in) in size, but varying from 0.2 to 30 mm in the case of the marine Gigantocypris. The largest known freshwater species is Megalocypris princeps, which reach 8mm in length. In most cases, their bodies are flattened from side to side and protected by a bivalve-like valve or "shell" made of chitin, and often calcium carbonate. The family Entocytheridae and many planktonic forms do not have calcium carbonate. The hinge of the two valves is in the upper (dorsal) region of the body. Ostracods are grouped together based on shell and soft part morphology. While early work indicated the group may not be monophyletic and early molecular phylogeny was ambiguous on this front, recent combined analyses of molecular and morphological data suggested monophyly in analyses with broadest taxon sampling, but this monophyly had no or very little support. They have a wide range of diets, and the class includes carnivores, herbivores, scavengers and filter feeders, but most ostracods are deposit feeders.

<span class="mw-page-title-main">Luciferin</span> Class of light-emitting chemical compounds

Luciferin is a generic term for the light-emitting compound found in organisms that generate bioluminescence. Luciferins typically undergo an enzyme-catalyzed reaction with molecular oxygen. The resulting transformation, which usually involves breaking off a molecular fragment, produces an excited state intermediate that emits light upon decaying to its ground state. The term may refer to molecules that are substrates for both luciferases and photoproteins.

<span class="mw-page-title-main">Firefly luciferase</span>

Firefly luciferase is the light-emitting enzyme responsible for the bioluminescence of fireflies and click beetles. The enzyme catalyses the oxidation of firefly luciferin, requiring oxygen and ATP. Because of the requirement of ATP, firefly luciferases have been used extensively in biotechnology.

<span class="mw-page-title-main">Firefly luciferin</span> Chemical compound

Firefly luciferin is the luciferin, or light-emitting compound, used for the firefly (Lampyridae), railroad worm (Phengodidae), starworm (Rhagophthalmidae), and click-beetle (Pyrophorini) bioluminescent systems. It is the substrate of luciferase, which is responsible for the characteristic yellow light emission from many firefly species.

<span class="mw-page-title-main">Bioluminescence imaging</span>

Bioluminescence imaging (BLI) is a technology developed over the past decades (1990's and onward). that allows for the noninvasive study of ongoing biological processes Recently, bioluminescence tomography (BLT) has become possible and several systems have become commercially available. In 2011, PerkinElmer acquired one of the most popular lines of optical imaging systems with bioluminescence from Caliper Life Sciences.

In enzymology, a Cypridina-luciferin 2-monooxygenase (EC 1.13.12.6) is an enzyme that catalyzes the chemical reaction

In enzymology, an Oplophorus-luciferin 2-monooxygenase, also known as Oplophorus luciferase is a luciferase, an enzyme, from the deep-sea shrimp Oplophorus gracilirostris [2], belonging to a group of coelenterazine luciferases. Unlike other luciferases, it has a broader substrate specificity [3,4,6] and can also bind to bisdeoxycoelenterazine efficiently [3,4]. It is the third example of a luciferase to be purified in lab [2]. The systematic name of this enzyme class is Oplophorus-luciferin:oxygen 2-oxidoreductase (decarboxylating). This enzyme is also called Oplophorus luciferase.

In enzymology, a Watasenia-luciferin 2-monooxygenase (EC 1.13.12.8) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Osamu Shimomura</span> Japanese organic chemist and marine biologist (1928–2018)

Osamu Shimomura was a Japanese organic chemist and marine biologist, and professor emeritus at Marine Biological Laboratory (MBL) in Woods Hole, Massachusetts and Boston University School of Medicine. He was awarded the Nobel Prize in Chemistry in 2008 for the discovery and development of green fluorescent protein (GFP) with two American scientists: Martin Chalfie of Columbia University and Roger Tsien of the University of California-San Diego.

<span class="mw-page-title-main">Coelenterazine</span> Chemical compound

Coelenterazine is a luciferin, a molecule that emits light after reaction with oxygen, found in many aquatic organisms across eight phyla. 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.

Photoproteins are a type of enzyme produced by bioluminescent organisms. They add to the function of the luciferins whose usual light-producing reaction is catalyzed by the enzyme luciferase.

<i>Vargula hilgendorfii</i> Species of seed shrimp

Vargula hilgendorfii, sometimes called the sea-firefly and one of three bioluminescent species known in Japan as umi-hotaru (海蛍), is a species of ostracod crustacean. It is the only member of genus Vargula to inhabit Japanese waters; all other members of its genus inhabit the Gulf of Mexico, the Caribbean Sea, and waters off the coast of California. V. hilgendorfii was formerly more common, but its numbers have fallen significantly.

<span class="mw-page-title-main">John Woodland Hastings</span>

John Woodland "Woody" Hastings, was a leader in the field of photobiology, especially bioluminescence, and was one of the founders of the field of circadian biology. He was the Paul C. Mangelsdorf Professor of Natural Sciences and Professor of Molecular and Cellular Biology at Harvard University. He published over 400 papers and co-edited three books.

<span class="mw-page-title-main">E. Newton Harvey</span> American zoologist (1887–1959)

Edmund Newton Harvey was an American zoologist. He was acknowledged as one of the leading authorities on bioluminescence. He won the Rumford Prize in 1947 and was a member of the National Academy of Sciences, the American Philosophical Society, and the American Academy of Arts and Sciences in 1929.

Yoshimasa Hirata was a Japanese organic chemist.

<span class="mw-page-title-main">Scintillon</span>

Scintillons are small structures in cytoplasm that produce light. Among bioluminescent organisms, only dinoflagellates have scintillons.

<span class="mw-page-title-main">Kleptoprotein</span>

A kleptoprotein is a protein which is not encoded in the genome of the organism which uses it, but instead is obtained through diet from a prey organism. Importantly, a kleptoprotein must maintain its function and be mostly or entirely undigested, drawing a distinction from proteins that are digested for nutrition, which become destroyed and non-functional in the process.

Vargula tsujii is a bioluminescent cypridinid ostracod found in southern California. It feeds on dead and decaying fish and invertebrates. Vargula tsujii is an important prey item of the plainfin midshipman fish, as it is the source of luciferin for the bioluminescence seen in the fish.

References

  1. Campbell AK, Herring PJ (1990). "Imidazolopyrazine bioluminescence in copepods and other marine organisms". Marine Biology. Springer Science and Business Media LLC. 104 (2): 219–225. doi:10.1007/bf01313261. ISSN   0025-3162. S2CID   84250053.
  2. Morin JG (2011). "Based on a review of the data, use of the term 'cypridinid' solves the Cypridina/Vargula dilemma for naming the constituents of the luminescent system of ostracods in the family Cypridinidae". Luminescence. Wiley. 26 (1): 1–4. doi:10.1002/bio.1282. ISSN   1522-7235. PMID   19862683.
  3. Shimomura, O. (2006). Bioluminescence: Chemical Principles and Methods. World Scientific Publishing. ISBN   978-981-256-801-4.
  4. Anderson, RS (1935). "Studies on Bioluminescence : II. the Partial Purification of Cypridina Luciferin". The Journal of General Physiology. 19 (2): 301–5. doi:10.1085/jgp.19.2.301. PMC   2141430 . PMID   19872927.
  5. Shimomura, O, Goto, T, Hirata, Y (1957). "Crystalline Cypridina Luciferin" (PDF). Bulletin of the Chemical Society of Japan. 30 (8): 929–933. doi: 10.1246/bcsj.30.929 . hdl:10069/20882.{{cite journal}}: CS1 maint: overridden setting (link)
  6. Kishi Y, Goto, T, Hirata Y, Shiromura O, Johnson FH (1966). "Cypridina bioluminescence. I. Structure of Cypridina luciferin". Tetrahedron Lett. 7 (29): 3427–3436. doi:10.1016/S0040-4039(01)82806-9.{{cite journal}}: CS1 maint: overridden setting (link)
  7. Oba, Y, Kato, S, Ojika, M, Inouye, S (2002). "Biosynthesis of luciferin in the sea firefly, Cypridina hilgendorfii: l-tryptophan is a component in Cypridina luciferin". Tetrahedron Letters. 43 (12): 2389–2392. doi:10.1016/S0040-4039(02)00257-5.{{cite journal}}: CS1 maint: overridden setting (link)
  8. Thompson EM, Nagata S, Tsuji FI (1989). "Cloning and expression of cDNA for the luciferase from the marine ostracod Vargula hilgendorfii". Proceedings of the National Academy of Sciences . 86 (17): 6567–71. Bibcode:1989PNAS...86.6567T. doi: 10.1073/pnas.86.17.6567 . PMC   297885 . PMID   2771943.
  9. "Luciferase Reporters". thermofisher.com.