|2D PASS solid-state 15-NMR spectrum (bottom) and cross-polarization magic angle spinning 15N solid-state NMR spectrum of tetracetyl riboflavin labeled with 15N at positions N1, N3 and N5. For details, see Koder et al. 2006.
Other events were unforeseen, however, such as Miller having to leave her first postdoctoral position at MIT because her lab ran out of funding, forcing her to scramble to find a new lab to work in. This situation was made more difficult by the facts that her husband had just gotten a job in the Boston area and that Miller wasn’t a U.S. citizen and would have to leave the country if she didn’t find a U.S. Immigration and Naturalization Service-acceptable position very quickly.
And, while Miller did secure a position at Brandeis, two years later the “two-body problem” became an issue again. After many unsuccessful attempts at finding a suitable destination with her husband, Miller eventually received a job offer she simply could not refuse: assistant professor in the Johns Hopkins University chemistry department.
Although her long-distance “e-marriage” was trying, Miller had a fantastic time at Hopkins. “I had a chance to launch some very exciting studies and to work with fabulous colleagues; I would have loved to have been able to stay permanently.” Despite the best efforts by her colleagues, the university couldn’t find a way to open up a spot in the physics department for her husband. “After eight years, our family had reached a point where our first child was ready to start school, and we just had to be in the same city.”
That led Miller to a difficult professional decision— relocating her lab to the University of Kentucky in 1999 so her family could be together.
Heading into Orbit
While the nature of the projects in Miller’s group at the University of Kentucky varies to exploit the composition and interests of her lab members, she maintains an overall theme of combining principles of biophysics and spectroscopy to examine protein control over cofactor reactivity.
The lab focuses on two enzyme types: superoxide dismutases and enzymes that use flavins as cofactors. Superoxide dismutases, which metabolize toxic superoxide ions (O2-), regulate the reactivity of potentially reactive chemical species and are fairly well studied, providing a firm foundation for detailed studies of fundamental questions.
“That is not to say superoxide dismutase has no more new stories to tell, because it certainly has,” Miller says, noting some exciting work in which her lab provided the first mechanistic explanation as to why iron- or manganese-containing superoxide dismutases become inactive if their cofactor is exchanged with the opposing ion, even though the three-dimensional structures of the two enzyme types are basically superimposable.