Scientists from Brno are looking for a way to sustainable lighting with the sea lamprey
The research of Brno scientists from the Loschmidt laboratories could one day bring about a similarly revolutionary change as the invention of the light bulb once caused. At the molecular level, they described and clarified the lighting mechanism of renilla purple, a sea glow. It is in animals with the ability of bioluminescence, i.e. the production of “cold” light, that mankind could be inspired in the search for ways to more sustainable and efficient lighting. The scientific journal Nature Catalysis reported on the research.
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Demonstration of cold light production
| Photo: CTK
“Luminescent enzymes could be used in our everyday lives, and not only in laboratories, where they are normally used. And precisely because we have mapped the bioluminescence process in detail at the molecular level, we are several steps closer to this. When the light bulb is lit, it is released heat, while luciferases do not release heat and can convert energy into light very efficiently. Our discovery represents a luminous revolution,” said biologist Martin Marek in a press release.
Luciferases are enzymes that enable bioluminescence in animals, such as fireflies. But cold light is also produced by organisms on the bottom of the sea, including purple renilla.
Brno scientists showed where and how the energy-rich substrate, so-called luciferin, binds in the enzyme molecule. Using methods of structural biology and spectroscopic measurements, they mapped the enzymatic oxidation of luciferin and its transformation into an energy-rich intermediate, the breakdown of which produces a visible blue flash.
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In their work using protein engineering methods, the scientists also reconstructed the “ancestor” of today’s renilla violet luciferase enzyme, thus uncovering the secret of its evolution. It was said to be “work like clockwork”. “This will now allow us to push the new luciferases even further and make their lighting even more efficient,” said another researcher, Martin Toul.
Now the scientists want to find out how long the enzyme can glow without interruption. So far, in laboratory conditions, luciferase has lit up a test tube for 48 hours. “The limitation here remains our lack of knowledge of how living organisms synthesize the energy-rich luciferin. Just as a nuclear reactor needs fuel in the form of enriched uranium, luciferases also need fuel for their operation, and that is exactly what luciferin is,” explained Marek.
Scientists have mastered methods to synthesize luciferins chemically in the laboratory, but the process is economically inefficient for practical use. “We need to uncover the biosynthetic pathways leading to the formation of luciferins and their recycling in cells in order to be able to construct a genetically coded and energy-independent light source,” outlined Marek.
Loschmidt’s protein engineering laboratories fall under the Recetox Center of the Faculty of Science of Masaryk University in Brno.