Amy C. Rosenzweig

Northwestern University

Primary Section: 14, Chemistry
Secondary Section: 21, Biochemistry
Membership Type: Member (elected 2017)


Amy Rosenzweig is the Weinberg Family Distinguished Professor of Life Sciences in the Departments of Molecular Biosciences and of Chemistry at Northwestern University. She is a bioinorganic chemist and structural biologist, known particularly for her studies of methane-oxidizing enzymes. Rosenzweig has also contributed broadly to understanding metal homeostasis and metalloenzyme function on the molecular level. Born and raised in Pittsburgh, Pennsylvania, she received a BA in chemistry from Amherst College (1988) and a PhD in inorganic chemistry from Massachusetts Institute of Technology (1994), working with Stephen J. Lippard. Rosenzweig is a fellow of the American Academy of Arts and Sciences (2014) and a member of the National Academy of Sciences (2017). Her awards include the Royal Society of Chemistry Joseph Chatt Award (2014), the American Chemical Society Nobel Laureate Signature Award for Graduate Education (2006), an Honorary Doctor of Science Degree from Amherst College (2005), and a MacArthur Fellowship (2003).

Research Interests

Amy Rosenzweig's laboratory uses biochemical, biophysical, X-ray crystallographic, spectroscopic, and omic approaches to attack problems at the forefront of bioinorganic chemistry. Areas of interest include biological methane oxidation, metal uptake and transport, and oxygen activation by metalloenzymes. A major project focuses on the particulate, membrane-bound methane monooxygenase (pMMO), with emphasis on elucidating the atomic details of the copper active site, understanding the mechanisms of dioxygen activation and methane oxidation, and probing the enzyme's function within the larger context of methanotroph physiology. In related work, the laboratory is studying bacterial copper acquisition by methanobactins, including how these novel natural products are biosynthesized and transported. Finally, the laboratory is investigating a range of membrane-bound transporters and soluble proteins involved in cellular transition metal handling.

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