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David H. Russell, 65, a professor and head of the chemistry department at Texas A&M University, is being honored for his many contributions to the development of mass spectrometry instrumentation and methods for identification and characterization of complex biological molecules.
Russell credits his undergraduate qualitative organic lab instructor, the late Frank Setliff, for sparking his interest in mass spectrometry. “Problem solving has always attracted me, and finding out that the identity of an unknown compound could be established by a combination of chemical reactions and spectroscopic techniques hooked me from day one,” Russell says. “Mass spectrometry and the potential it possessed for such problem solving was a real eye-opener.”
Russell received his B.S. in chemistry from the University of Arkansas, Little Rock, in 1974. He then studied with Michael L. Gross at the University of Nebraska, Lincoln, earning a Ph.D. in chemistry in 1978. Russell subsequently worked as a research scientist at Oak Ridge National Laboratory from 1978 to 1980. Since 1980, he has been on the faculty of Texas A&M.
Throughout his career, Russell has focused on developing methods and technology for characterizing the structure of gas-phase ionic species. In that work, he has advanced many types of mass analyzers, including time-of-flight, Fourier transform ion cyclotron resonance (FT-ICR), and ion mobility-mass spectrometry.
“David’s innovations in the late-eighties to mid-nineties have become the foundation for the analysis of intact high-mass biomolecules using FT-ICR,” says Ronald D. Macfarlane, a colleague at Texas A&M. Russell designed cells that hold the record for trapping high-mass ions (>150,000 mass-to-charge ratio), Macfarlane says. In addition, Russell was a pioneer in combining matrix-assisted laser desorption/ionization (MALDI) with tandem mass spectrometry.
“He is not merely doing great mass spectrometry, he is changing the field of mass spectrometry,” says Kermit K. Murray, a professor at Louisiana State University, Baton Rouge, who was a postdoctoral researcher in Russell’s lab in the early 1990s. “He has pushed the limits of mass spectrometer performance and has done things that few others have imagined: MALDI of aerosols, MALDI in an ICR cell, ICR of large proteins, innovations in ICR cells, and ion-molecule reactions.”
Much of that work has been done to apply mass spectrometry to biological systems. Biological and proteomics mass spectrometry “has been a major driving force behind many developments in mass spectrometry,” Russell says. “I’ve wanted to be a participant in such an exciting period.”
He is particularly interested in combining ion mobility and mass spectrometry to better understand the effect of solvent on the structure and conformation of peptides, especially amphipathic peptides. “This is an area where mass spectrometry and ion mobility can provide answers that are difficult, if not impossible, to obtain using other techniques,” Russell says.
Despite his many scientific contributions, Russell considers his most important contribution to be the training of a new generation of young scientists. “The other things will be lost in the noise because the advances in chemistry are so rapid and the impact of one’s contributions is quickly lost or forgotten,” he says.
Russell will deliver the award address before the ACS Division of Analytical Chemistry.