Luciferase

JAMS Meeting Report – April 2012
by Thomas Jeffries
 
There was a good turnout on ANZAC day eve for three interesting talks, pizza and free local beer.
 
Kicking off the evening was John Lee, from the University of Georgia, with his ambitiously titled talk “Bioluminescence: The First 3000 Years”.  After a historical introduction to the long running observation of bioluminescence, via the discovery in 1672 that oxygen was necessary for bacterial luminescence, John told us how it was determined that bioluminescence is an enzyme mediated chemical reaction involving “luciferase” and "luciferine". In the modern age of biochemistry it was determined that ATP is the substrate in this reaction.  Following the elucidation of the structure of firefly luciferase in 1959, modern techniques (i.e. picosecond dynamic fluorescence spectroscopy and NMR) have allowed researchers to uncover the enzymes and processes involved in bioluminescence.  One of the most important of these enzymes Green-fluorescent protein (GFP) was discovered in jellyfish by Shimomura (who evidently has a lab at his house!) and led to his Nobel prize in 2008.  Due to GFP’s widespread use in research, it is regarded as one of the most important proteins in science.
 

Event Date: 
Tuesday, April 24, 2012 - 18:00 - 18:15
Institution: 
University of Georgia
Title: 

Bioluminescence: The First 3000 Years

Abstract: 

Bioluminescence along with astronomy, is one of the oldest subjects of scientific investigation.  Light from fireflies is mentioned in ancient Chinese poetry and later more systematic studies are in the writings of Aristotle and Pliny the Elder.  In the modern era, Robert Boyle in a 1672 Proc. Roy. Soc. paper, reported the requirement of bacterial bioluminescence for air, now known to be oxygen.  His paper contained the first published Table of experimental results.  In 1876 Dubois reported that the living light from the bioluminescent clam, could be extracted into solution.  He showed that bioluminescence was just a chemical reaction, an enzyme and substrate, which he dubbed “luciferase” and "luciferine".  In 1947, McElroy reported that Dubois' substrate was actually ATP.  Genuine firefly luciferin was not purified and structurally characterized until 1959.  In 1962, Shimomura noted the presence of a “green protein” in extracts of the bioluminescent jellyfish.  10 years later this was named “Green-fluorescent protein” (GFP), now the most famous protein in Science and the basis of Shimomura’s Nobel prize in 2008.
In the last two decades we have applied biophysical methods: picosecond dynamic fluorescence spectroscopy, NMR, and structural biology, for uncovering bioluminescence mechanisms.  I will show how this most primitive organism, the jellyfish, early discovered the most advanced physics, quantum correlation, to generate its characteristic green bioluminescence.

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