Bioluminescence

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Not to be confused with Iridescence, Structural coloration, or Phosphorescence.

Flying and glowing firefly, Photinus pyralis

Female glowworm, Lampyris noctiluca

Male and female of the species Lampyris noctiluca mating. The female of this species is a larviform and has no wings, unlike
the male.

Video of a bioluminescent beetle Elateroidea
 Bioluminescence is the production and emission of light by a living organism. 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.
In a general sense, the principal chemical reaction in bioluminescence involves a light-emitting
molecule and an enzyme, generally called luciferin and luciferase, respectively. Because these are
generic names, luciferins and luciferases are often distinguished by the species or group,
e.g. firefly luciferin. In all characterized cases, the enzyme catalyzes the oxidation of the luciferin.
In some species, the luciferase requires other cofactors, such as calcium or magnesium ions, and
sometimes also the energy-carrying molecule adenosine triphosphate (ATP). In evolution, luciferins
vary little: one in particular, coelenterazine, is found in 11 different animal phyla, though in some of
these, the animals obtain it through their diet. Conversely, luciferases vary widely between different
species, which is evidence that bioluminescence has arisen over 40 times in evolutionary history.
Both Aristotle and Pliny the Elder mentioned that damp wood sometimes gives off a glow. Many
centuries later Robert Boyle showed that oxygen was involved in the process, in both wood and
glowworms. It was not until the late nineteenth century that bioluminescence was properly
investigated. The phenomenon is widely distributed among animal groups, especially in marine
environments. On land it occurs in fungi, bacteria and some groups of invertebrates,
including insects.
The uses of bioluminescence by animals include counter-illumination camouflage, mimicry of other
animals, for example to lure prey, and signalling to other individuals of the same species, such as
to attract mates. In the laboratory, luciferase-based systems are used in genetic engineering and
biomedical research. Researchers are also investigating the possibility of using bioluminescent
systems for street and decorative lighting, and a bioluminescent plant has been created. [1]

Contents

 1History
 2Evolution
 3Chemical mechanism
 4Distribution
o 4.1Pelagic zone
 4.1.1Bacterial symbioses
o 4.2Benthic zone
 5Uses in nature
o 5.1Counter-illumination camouflage
o 5.2Attraction
o 5.3Defence
o 5.4Warning
o 5.5Communication
o 5.6Mimicry
o 5.7Illumination
 6Biotechnology
o 6.1Biology and medicine
o 6.2Light production
 7See also
 8Notes
 9References
 10Further reading
 11External links

History[edit]
Before the development of the safety lamp for use in coal mines, dried fish skins were used in
Britain and Europe as a weak source of light. [2] This experimental form of illumination avoided the
necessity of using candles which risked sparking explosions of firedamp.[3] Another safe source of
illumination in mines was bottles containing fireflies. [4] In 1920, the American zoologist E. Newton
Harvey published a monograph, The Nature of Animal Light, summarizing early work on
bioluminescence. Harvey notes that Aristotle mentions light produced by dead fish and flesh, and
that both Aristotle and Pliny the Elder (in his Natural History) mention light from damp wood. He
also records that Robert Boyle experimented on these light sources, and showed that both they
and the glowworm require air for light to be produced. Harvey notes that in 1753, J. Baker identified
the flagellate Noctiluca "as a luminous animal" "just visible to the naked eye", [5] and in 1854 Johann
Florian Heller (1813–1871) identified strands (hyphae) of fungi as the source of light in dead wood.
[6]

Tuckey, in his posthumous 1818 Narrative of the Expedition to the Zaire, described catching the
animals responsible for luminescence. He mentions pellucids, crustaceans (to which he ascribes
the milky whiteness of the water), and cancers (shrimps and crabs). Under the microscope he
described the "luminous property" to be in the brain, resembling "a most brilliant amethyst about
the size of a large pin's head".[7]
Charles Darwin noticed bioluminescence in the sea, describing it in his Journal:
While sailing in these latitudes on one very dark night, the sea presented a wonderful and most
beautiful spectacle. There was a fresh breeze, and every part of the surface, which during the day
is seen as foam, now glowed with a pale light. The vessel drove before her bows two billows of
liquid phosphorus, and in her wake she was followed by a milky train. As far as the eye reached,
the crest of every wave was bright, and the sky above the horizon, from the reflected glare of these
livid flames, was not so utterly obscure, as over the rest of the heavens. [8]
Darwin also observed a luminous "jelly-fish of the genus Dianaea" [8] and noted that "When the
waves scintillate with bright green sparks, I believe it is generally owing to minute crustacea. But
there can be no doubt that very many other pelagic animals, when alive, are phosphorescent." [8] He
guessed that "a disturbed electrical condition of the atmosphere" [8] was probably responsible.
Daniel Pauly comments that Darwin "was lucky with most of his guesses, but not here", [9] noting
that biochemistry was too little known, and that the complex evolution of the marine animals
involved "would have been too much for comfort". [9]
Osamu Shimomura isolated the photoprotein aequorin and its cofactor coelenterazine from the crystal jelly Aequorea
victoria in 1961.[10]

Bioluminescence attracted the attention of the United States Navy in the Cold War, since
submarines in some waters can create a bright enough wake to be detected; a German submarine
was sunk in the First World War, having been detected in this way. The navy was interested in
predicting when such detection would be possible, and hence guiding their own submarines to
avoid detection.[11]
Among the anecdotes of navigation by bioluminescence is one recounted by the Apollo
13 astronaut Jim Lovell, who as a navy pilot had found his way back to his aircraft
carrier USS  Shangri-La when his navigation systems failed. Turning off his cabin lights, he saw the
glowing wake of the ship, and was able to fly to it and land safely. [12]
The French pharmacologist Raphaël Dubois carried out work on bioluminescence in the late
nineteenth century. He studied click beetles (Pyrophorus) and the marine bivalve mollusc Pholas
dactylus. He refuted the old idea that bioluminescence came from phosphorus, [13][a] and
demonstrated that the process was related to the oxidation of a specific compound, which he
named luciferin, by an enzyme.[15] He sent Harvey siphons from the mollusc preserved in sugar.
Harvey had become interested in bioluminescence as a result of visiting the South Pacific and
Japan and observing phosphorescent organisms there. He studied the phenomenon for many
years. His research aimed to demonstrate that luciferin, and the enzymes that act on it to produce
light, were interchangeable between species, showing that all bioluminescent organisms had a
common ancestor. However, he found this hypothesis to be false, with different organisms having
major differences in the composition of their light-producing proteins. He spent the next 30 years
purifying and studying the components, but it fell to the young Japanese chemist Osamu
Shimomura to be the first to obtain crystalline luciferin. He used the sea firefly Vargula hilgendorfii,
but it was another ten years before he discovered the chemical's structure and published his 1957
paper Crystalline Cypridina Luciferin.[16] Shimomura, Martin Chalfie, and Roger Y. Tsien won the
2008 Nobel Prize in Chemistry for their 1961 discovery and development of green fluorescent
protein as a tool for biological research.[17]
Harvey wrote a detailed historical account on all forms of luminescence in 1957. [18] An updated book
on bioluminescence covering also the twentieth and early twenty-first century was published
recently.[19][20]

Evolution[edit]
In 1932 E. N. Harvey was among the first to propose how bioluminescence could have evolved.
[21]
 In this early paper, he suggested that proto-bioluminescence could have arisen from respiratory
chain proteins that hold fluorescent groups. This hypothesis has since been disproven, but it did
lead to considerable interest in the origins of the phenomenon. Today, the two prevailing
hypotheses (both concerning marine bioluminescence) are those put forth by Howard Seliger in
1993 and Rees et al. in 1998.[22][23]
Seliger's theory identifies luciferase enzymes as the catalyst for the evolution of bioluminescent
systems. It suggests that the original purpose of luciferases was as mixed-function oxygenases. As
the early ancestors of many species moved into deeper and darker waters natural selection
favored the development of increased eye sensitivity and enhanced visual signals. [24] If selection
were to favor a mutation in the oxygenase enzyme required for the breakdown of pigment
molecules (molecules often associated with spots used to attract a mate or distract a predator) it
could have eventually resulted in external luminescence in tissues. [22]
Rees et al. use evidence gathered from the marine luciferin coelenterazine to suggest that
selection acting on luciferins may have arisen from pressures to protect oceanic organisms from
potentially deleterious reactive oxygen species (e.g. H 2O2 and O2− ). The functional shift from
antioxidation to bioluminescence probably occurred when the strength of selection for antioxidation
defense decreased as early species moved further down the water column. At greater depths
exposure to ROS is significantly lower, as is the endogenous production of ROS through
metabolism.[23]
While popular at first, Seliger's theory has been challenged, particularly on the biochemical and
genetic evidence that Rees examines. What remains clear, however, is that bioluminescence has
evolved independently at least 40 times.[25] Bioluminescence in fish began at least by
the Cretaceous period. About 1,500 fish species are known to be bioluminescent; the capability
evolved independently at least 27 times. Of these, 17 involved the taking up of bioluminous
bacteria from the surrounding water while in the others, the intrinsic light evolved through chemical
synthesis. These fish have become surprisingly diverse in the deep ocean and control their light
with the help of their nervous system, using it not just to lure prey or hide from predators, but also
for communication.[26][27]
All bioluminescent organisms have in common that the reaction of a "luciferin" and oxygen is
catalyzed by a luciferase to produce light. [28] McElroy and Seliger proposed in 1962 that the
bioluminescent reaction evolved to detoxify oxygen, in parallel with photosynthesis. [29]
Thuesen, Davis et al. showed in 2016 that bioluminescence has evolved independently 27 times
within 14 fish clades across ray-finned fishes.[26]

Chemical mechanism[edit]
Main article: Luciferase

Protein structure of the luciferase of the firefly Photinus pyralis. The enzyme is a much larger molecule than luciferin.

Bioluminescence is a form of chemiluminescence where light energy is released by a chemical

reaction. This reaction involves a light-emitting pigment, the luciferin, and a luciferase, the enzyme
component.[30] Because of the diversity of luciferin/luciferase combinations, there are very few
commonalities in the chemical mechanism. From currently studied systems, the only unifying
mechanism is the role of molecular oxygen, which provides chemical energy;[31] often there is a
concurrent release of carbon dioxide (CO2). For example, the firefly luciferin/luciferase reaction
requires magnesium and ATP and produces CO2, adenosine monophosphate (AMP)
and pyrophosphate (PP) as waste products. Other cofactors may be required, such as calcium
(Ca2+) for the photoprotein aequorin, or magnesium (Mg2+) ions and ATP for the firefly luciferase.
[32]
 Generically, this reaction can be described as:
 Luciferin + O2 Oxyluciferin + light energy

Coelenterazine is a luciferin found in many different marine phyla from comb jellies to vertebrates. Like all luciferins,
it is oxidised to produce light.

Instead of a luciferase, the jellyfish Aequorea victoria makes use of another type of protein

called a photoprotein, in this case specifically aequorin.[33] When calcium ions are added,
rapid catalysis creates a brief flash quite unlike the prolonged glow produced by luciferase. In a
second, much slower step, luciferin is regenerated from the oxidized (oxyluciferin) form,
allowing it to recombine with aequorin, in preparation for a subsequent flash. Photoproteins are
thus enzymes, but with unusual reaction kinetics.[34] Furthermore, some of the blue light
released by aequorin in contact with calcium ions is absorbed by a green fluorescent protein,
which in turn releases green light in a process called resonant energy transfer.[35]
Overall, bioluminescence has arisen over 40 times in evolutionary history. [30] In evolution,
luciferins tend to vary little: one in particular, coelenterazine, is the light emitting pigment for
nine phyla (groups of very different organisms), including
polycystine radiolaria, Cercozoa (Phaeodaria), protozoa, comb
jellies, cnidaria including jellyfish and corals, crustaceans, molluscs, arrow
worms and vertebrates (ray-finned fish). Not all these organisms synthesise coelenterazine:
some of them obtain it through their diet.[30] Conversely, luciferase enzymes vary widely and
tend to be different in each species.[30]