|
|
| Name |
Rosenzweig, Amy C. |
| Location
|
Northwestern University - Evanston |
| Primary Field
|
Chemistry |
| Secondary Field
|
Biochemistry |
 Election Citation
|
|
Rosenzweig is a leader in the study of metalloprotein structure and function. Her pioneering studies of particulate methane monooxygenase identified and characterized its copper active site. More broadly, she has provided key insights into metal-protein recognition, metal transfer between protein partners, and metal translocation across membranes. |
|
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. |
|
|
|