Amy Rosenzweig

Her current research interests include structural biology and bioinorganic chemistry, metal uptake and transport, oxygen activation by metalloenzymes, and characterization of membrane protein.

At MIT, Rosenzweig worked under the supervision of Stephen J. Lippard where she pioneered the structural studies of the hydroxylase component of methane monooxygenase from methyloccous capsulatus.

In the following years, she made major advances in determining the enzyme's bioactivity and chemical constitution, including vast contributions to research on the metal-coordinated active site.

[3][4] The currently proposed mechanism for sMMO involves an Iron (II) coordination complex that is twice oxidized to form a metalloperoxide species.

"[2] In her work with pMMOs, Rosenzweig elucidated the molecular basis for safe handling of potentially toxic metal ions through direct handoff between protein partners.