Issue Date: January 23, 2012
Alfred Bader Award In Bioinorganic Or Bioorganic Chemistry
Sponsored by the Alfred R. Bader Fund
Ask chemists how they got interested in chemistry and you often hear about how they played with chemistry kits or had an inspirational teacher. But for Brian M. Hoffman, chemistry professor at Northwestern University, the interest came as a result of an uninspiring high school physics class.
“At my high school, you took physics as a junior and chemistry as a senior if you were interested in science,” Hoffman says. “I had a charming rogue of a teacher, who gave me a good grade, but at the end of the year I was chagrined to realize I hadn’t learned a bloody thing.”
Determined not to waste another year sitting in a science class learning nothing, Hoffman vowed to learn something in his chemistry class, regardless of the teacher. “I had a different charming rogue for a teacher, who taught us nothing, but this time I wasn’t going to be cheated so I worked really hard. Somehow that got me on the chemistry train, and I never got off,” he says.
Hoffman went on to earn a B.S. from the University of Chicago in 1962 and a Ph.D. from California Institute of Technology with Harden M. McConnell in 1966, both in chemistry. After a postdoctoral year at Massachusetts Institute of Technology with Alexander Rich, he joined Northwestern in 1967. In the decades that followed, Hoffman has become a pioneer in the field of bioinorganic chemistry. It is for his work using electron-nuclear double resonance (ENDOR) to study metalloenzymes that he is now being honored.
“When I started using this tool, the technical problems of applying it to metalloenzymes hadn’t been solved,” Hoffman explains. “It wasn’t clear how you would systematically use this tool to understand enzyme structure and mechanism,” he notes, adding that today, researchers worldwide are involved in this area.
The ENDOR work in Hoffman’s lab is currently focused on understanding numerous enzymes, particularly nitrogenase. In addition to the ENDOR studies, his lab also investigates electron transfer within protein complexes and the synthesis of novel porphyrazine macrocycles. He has more than 540 publications to his credit.
“Hoffman has made wide-ranging contributions to advancing the chemistry enterprise through his work in bioinorganic chemistry, in particular through his development of ENDOR spectroscopy as essential in the determination of metalloenzyme catalytic mechanisms,” says Joan S. Valentine, a chemistry professor at the University of California, Los Angeles. “His laboratory has been decisively involved with all the major metalloenzymes, including nitrogenase, cytochrome oxidase, hydrogenases, peroxidases, mono- and dioxygenases, and FeS centers including ‘radical S-adenosylmethionine’ enzymes.”
Hoffman has not only identified and characterized the structures of key intermediates, but he has also “devised and implemented novel kinetic methods of exploring their reactivity,” adds Judith P. Klinman, a chemistry professor at UC Berkeley.
Hoffman has won numerous awards, including the Royal Society of Chemistry’s Bruker Prize in 1997, the Russian Academy of Sciences’ Zavoisky Prize in 2007, and the Max Planck Society’s Frontiers in Biological Chemistry Award in 2008. He is a fellow of the American Association for the Advancement of Science, the American Academy of Arts & Sciences, and the International Society of Magnetic Resonance and is also a member of the National Academy of Sciences.
Hoffman will present the award address before the ACS Division of Inorganic Chemistry.
- Chemical & Engineering News
- ISSN 0009-2347
- Copyright © American Chemical Society