© JASON DAILEY PHOTOWhen she was an undergraduate studying marine biology at Texas A&M University at Galveston, Emily Scott received a late-night phone call from her professor. A bunk had become available on a research boat bound for oxygen-depleted “dead zones” in the Gulf of Mexico, but it was leaving the next day. Scott jumped at the chance. Despite battling seasickness as she took course exams on board the ship, Scott enjoyed her first taste of hands-on science. “I was hooked, and I went back every chance I got,” she says.
Scott was interested in benthic invertebrates, in particular brittle stars, which have hemoglobin in their water vascular systems. That led to her fascination with heme proteins, which enfold a permanently bound iron-containing molecule and carry out a diverse range of biological functions.
METHODS: In 1995 Scott embarked on a PhD at Rice University in Houston, where she showed that the heme-encircling protein scaffolds of myoglobins from deep-diving whales are approximately 100 times more stable than those from terrestrial animals. “She was always willing try any new technique to solve a problem,” says John Olson, her supervisor at Rice.
But Scott knew that globins, the most well-studied heme proteins, were not the best area for a young scientist to make an impact. Instead, she decided to ...
