Nobel winning chemist Shimomura dies at 90; lauded for work

The bomber planes, he thought, had a certain beauty, flashing silver against the blue sky before dropping their explosive cargo on industrial plants near Nagasaki, Japan.

He watched them from a hill next to his own factory, where he was assigned to work on fighter-plane engines about 9 miles from town, and was following them one Thursday morning in August 1945 when they took an unusual route toward the center of the city.

“We were blinded for about 30 seconds,” Osamu Shimomura later remembered, recalling the U.S. atomic bomb blast that destroyed nearly half of Nagasaki. “Then, about 40 seconds after the flash, a loud sound and sudden change of air pressure followed. We were sure there was a huge explosion somewhere, but we didn’t know where.”

Dr. Shimomura, who was then 16, emerged from the attack shaken but physically unscathed. He went on to build an unlikely new life as a chemist, performing experiments that transformed scientists’ understanding of bioluminescence, in which living organisms produce and emit light, sometimes while surrounded by total darkness.

Recalling his first major achievement as a chemist in the mid-1950s, the crystallization of a substance that enables a small Japanese crustacean to glow, he once wrote: “Since the end of the war, my life had been dark, but this gave me hope for my future.”

Less than a decade later, Shimomura had uncovered an unusual protein within a beautiful, brightly glowing jellyfish — a discovery that earned him a one-third share of the Nobel Prize in chemistry and formed the basis of a powerful new scientific tool, enabling biologists to follow the intricate movements of cells and individual proteins.

He was 90 when he died Oct. 19 in Nagasaki, according to the Marine Biological Laboratory in Woods Hole, Mass., which announced the death but did not give a cause. Shimomura had served as a senior scientist at the institute from 1982 until his retirement in 2001, and was also a professor emeritus at the Boston University School of Medicine.

Friday Harbor jellyfish

Traveling during the summer to conduct field work, Shimomura studied bioluminescent fireworms in Bermuda, cave worms and limpets in New Zealand, and a plethora of glowing bacteria, twinkling fireflies and neon-colored squid and krill. His central discovery was centered on a North American jellyfish, Aequorea victoria, sometimes called the crystal jelly.

He was working at Princeton University when a colleague, the biologist Frank Johnson, brought the animals to his attention and suggested that Shimomura travel to Friday Harbor, where the jellyfish seemed to congregate in Puget Sound. The two men went there together in the summer of 1961, traveling across the country with a pair of research assistants — including Shimomura’s wife, Akemi — in a seven-day trip by station wagon.

In an autobiographical essay for the Nobel Prize, Shimomura wrote that they set up shop at Friday Harbor Laboratories, a field station run by the University of Washington, where “a constant stream of floating jellyfish passed along the side of the lab dock every morning and evening, riding with the tidal current.”

With a simple dip net, he and the Princeton team scooped up jellyfish one by one, using a pair of scissors — and later a “jellyfish cutting machine” — to eliminate unnecessary body parts. Skeptical residents asked Shimomura how he was planning to eat the jellyfish, doubtful that they were actually being used for research. But by the end of the summer, he and his team had taken samples from 10,000 of the creatures, enabling him to isolate a pair of luminescent proteins early the following year.

The first and most promising protein, aequorin, was later used as an indicator for calcium. The second –green fluorescent protein, or GFP, which appears fluorescent green under ultraviolet light — remained little known for more than two decades, until Martin Chalfie, a biological sciences professor at Columbia University, decided to use it in his work with a transparent roundworm.

“It didn’t take much to realize that if I put that fluorescent protein inside this transparent animal, I would be able to see the cells that were making it,” Chalfie told the New York Times in 2008. “And that’s what we set out to do.”