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Brian Hoffman Elected to National Academy of Sciences

April 25, 2006

EVANSTON, Ill. --- Brian M. Hoffman, professor of chemistry at Northwestern University, has been elected to the National Academy of Sciences.

He joins 72 new members and 18 foreign associates from 16 countries in recognition of their distinguished and continuing achievements in original research.

"Election to the Academy is considered one of the highest honors in American science and engineering," said Ralph Cicerone, president of the Academy.

The National Academy of Sciences is a private organization of scientists and engineers dedicated to the furtherance of science and its use for the general welfare.  It was established in 1863 by a congressional act of incorporation signed by Abraham Lincoln that calls on the Academy to act as an official adviser to the federal government, upon request, in any matter of science or technology.

Hoffman, who holds a joint appointment in biochemistry, molecular biology, and cell biology, conducts research involving electron-nuclear double resonance (ENDOR) study of metalloenzymes, long-range electron transfer between proteins, and new macro-cycles for solid-state and biomedical applications. ENDOR is a spectroscopic tool that provides structural information about the active-site structure of metalloenzymes, not merely in their resting states, but most importantly as the enzymes are converted to key catalytic intermediates. As a result this technique provides information that is essential in determining how physiologically vital metal centers actually work.

Hoffman's recent work has been particularly important in advancing understanding of the function of cytochrome P450, a liver enzyme important for the metabolism of many drugs, and of nitrogenase, the enzyme that in nature turns atmospheric nitrogen gas into bioavailable ammonia.

Electron transfer is a fundamental reaction in chemistry and biology. The study of electron transfer within physiological complexes begins without the knowledge of the geometry of binding or the rules for protein-protein recognition. Kinetic, nuclear magnetic resonance and calorimetric measurements of wild-type and mutant complexes are first used to study their protein-protein recognition, and when successful, provide information to enable probing the electron transfer itself.

Hoffman is synthesizing porphyrin variants with novel chemical and optical properties. These can be made to bind multiple metal ions and have potential uses in several areas including biomedical applications in imaging and therapy.

Hoffman has received the Royal Society of Chemistry Bruker Prize and the International EPR Society Gold Medal and is a fellow of the American Academy of Arts and Sciences and of the American Association for the Advancement of Science. He has held an Alfred P. Sloan Fellowship and an NIH Career Development Award and was the Dow Research Professor of Chemistry at Northwestern University from 1990-92.

He has served as chair of the Metals in Biology Gordon Research Conference and a member of the Council of Gordon Research Conferences, the editorial boards of “Journal of Magnetic Resonance” and “Journal of Bioinorganic Chemistry” and the editorial advisory board of the “Journal of the American Chemical Society.

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