Bioluminescence -- the peculiar ability of some organisms to behave like living night-lights -- has been “invented” dozens of times in evolutionary history and serves a variety of purposes, from attracting mates and luring prey to warding off predators. Its existence in fungi – a rare if not unique case of bioluminescence outside the animal and microbial worlds – has posed more of a mystery. But scientists may now be able to explain not only why certain mushrooms glow in the dark, but how – and in doing so they could be nearer to creating glowing trees as a novel form of street lighting. A team from the Institute of Bio-organic Chemistry in Moscow has teased apart the chemical structure of the fungal protein used to generate the ghostly glow of foxfire. They did it by the counterintuitive approach of looking for it in mushrooms that did not glow in the dark because it was here they thought the precursors of the bioluminescence substance, known as luciferin, might be more easily found – and they were right. According to their findings, the mechanism of fungal bioluminescence suggests the formation of luciferin from a certain precursor. It was established that the luciferin precursor is also present in non-luminous forest fungi, and more importantly it is about 100 times more abundant than in the biomass of luminous species. Therefore, it made sense to extract the precursor from non-luminous fungi. Russian scientists found that the bioluminescent fungi use a type of luciferin quite different from the eight other classes of molecule already chemically described in the animal and microbial worlds. He and his team effectively discovered the ninth luciferin, and the first to be found in the fungal-plant sphere of life. https://www.theguardian.com/science...-mushrooms-conservation-enviroment-bioscience
Fireflies, anglerfish, and other organisms produce the light-emitting pigment luciferin and the enzyme luciferase. Luciferin reacts with OXYGEN to create light: Coelenterazine is a luciferin found in many different marine phyla from comb jellies to vertebrates. Like all luciferins, it is OXIDIZED to produce light. Carbon dioxide (CO 2 ), adenosine monophosphate (AMP) and phosphate groups (PP) are released as waste products. Luciferase catalyzes the reaction, which may be mediated by cofactors such as calcium (Ca 2+ ) or magnesium (Mg 2+ ) ions, and for some types of luciferin (L) also the energy-carrying molecule adenosine triphosphate (ATP). The reaction can occur either inside or outside the cell. In bacteria such as Aliivibrio, the expression of genes related to bioluminescence is controlled by the lux operon. So glowing plant/tree( of Luciferin) needs O2 to produce light and if they trying to make glowing trees(of Lucifrin)as a novel form of street lighting then what about solar powered LED street light !! Luciferin-luciferase reactions are not the only way that organisms produce light. The parchment worm Chaetopterus (a marine Polychaete) makes use of another photoprotein, aequorin, instead of luciferase. When calcium ions are added, the aequorin's 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 oxidised (oxyluciferin) form, allowing it to recombine with aequorin, in readiness for a subsequent flash. Photoproteins are thus enzymes, but with unusual reaction kinetics. In the hydrozoan jellyfish Aequorea victoria, some of the blue light released by aequorin in contact with calcium ions is absorbed by green fluorescent protein; it in turn releases green light.
