Serendipity in Science and GFP

In 1959, a young scientist by the name of Osamu Shimomura joined the lab of Dr Frank Johnson in Princeton. He had been recruited because of his excellent work on the structure of luciferin in the crustacean Cypridina hilgendorfii in the lab of Dr Yoshimasa Hirata. Dr Johnson directed Dr Shimomura to work on the bioluminescence of the jellyfish Aequorea. Their aim was to try and extract the bioluminescent substance from the jellyfish. This did not come easily. The scientific wisdom at the time was that all bioluminescence resulted from the oxidation of luciferin by luciferase (this is exactly what happens in Cypridina), and so they started there. After several failed attempts, Dr Shimomura began to question this knowledge and began to look elsewhere; however Dr Johnson disagreed and continued to look for luciferin and luciferase. Dr Shimomura toiled on unsuccessfully; suddenly one day he had a brilliant idea. He knew that the amount of luminescent substance decreases if the luminescence reaction is active. He had previously tried unsuccessfully to inhibit this reaction. This time, he reasoned that if the fluorescent substance is a protein, he should be able to inhibit the reaction by changing the pH. So that's what he did, and finally succeeded in producing a cell free extract in a pH 4 buffer that did not fluoresce until neutralised by NaHCO3. What happened next was quite memorable. Shimomura threw his samples into the sink, only to be surprised by a bright blue flash. Water from a mini aquarium in the lab had leaked into the sink, which led him to believe that something in the water had caused the flash. He was able to identify that it was Ca2+ ions that were responsible. Shimomura went on to discover the proteins aequorin and gfp (green fluorescent protein), and was a co-recipient of the Nobel Prize in Chemistry in 2008 for “The Discovery and Development of GFP.”