PIPages
Labs

Gloria Borgstahl

University of Nebraska Medical Center, NE·Biochemistry

Every enzyme works through the exact positions of its atoms. Seeing that arrangement in three dimensions shows how the enzyme does its chemistry and how drugs might change what it does.

Fields

Biochemistry

Biophysics

Chemistry

Topics

structural biology

superoxide dismutase

MnSOD

Grants
3 known grants, through Apr 2027

What they work on

  1. Map the proton environment of human MnSOD, an antioxidant enzyme, in its resting reduced and oxidized manganese states, using neutron crystallography at Oak Ridge National Laboratory to locate hydrogen atoms.
  2. Determine proton positions in the product-inhibited Mn-peroxo complex and the superoxide-bound form of MnSOD to test whether protons travel from water molecules via amino acids to the buried manganese.
  3. Use spectroscopy on crystals to design and interpret neutron experiments, and computational chemistry on all-atom structures to test proposed proton- and electron-transfer mechanisms of MnSOD.
  4. Provide protein expression and purification, robotic crystallization, X-ray crystallography, small-angle X-ray scattering (SAXS) and NMR data collection to cancer center researchers determining macromolecular structures.
  5. Support research on basic cancer mechanisms, including genome instability, tumor signaling and cancer metabolism and cachexia, to identify potential biomarkers and treatment strategies.

More about the research

The research here centers on solving protein structures at atomic detail. A special focus is hydrogen atoms (protons), which standard methods struggle to see. The main research project examines how an antioxidant enzyme, manganese superoxide dismutase, works. The grants also support a shared structural biology facility and a cancer biology research program at the institution's cancer center.

Why it matters

Abnormal SOD activity appears in cancer, neurodegenerative diseases and cardiovascular dysfunction. An atom-by-atom picture of how MnSOD neutralizes superoxide could clarify its role in these diseases and guide the design of therapies that adjust its activity. The shared facility and cancer program support structure-based studies and basic cancer research that could lead to new biomarkers and treatment strategies for cancer patients.

Known grants

From NIH and NSF research grants. Labs often have other funding we can't see.

Deciphering the Enzymatic Mechanism of Superoxide Dismutase

NIH · Aug 2022 – Apr 2027

Structural Biology Shared Resource

NIH · Sep 1997 – Aug 2026

Cancer Biology Program

NIH · Sep 1997 – Aug 2026

Closest labs

Patrick Lombardi

Mount St. Mary's University, MD·Biochemistry

Identify the specific molecular contacts between the ASCC2 CUE domain, a small ubiquitin-binding module, and K63-linked polyubiquitin chains, using NMR spectroscopy to report on atom-level interactions.

Mark Lipke

Rutgers University-New Brunswick, NJ·Chemistry

Measure how water trapped inside redox-active porphyrin nanocages changes the acidity of acid-bearing guest molecules and their combined proton-electron transfer, using electrochemistry and 1H NMR to quantify water uptake.

Ellen Matson

University of Rochester, NY·Chemistry

Determine how hydrogen atoms are taken up at the surface of polyoxovanadate–alkoxide and –carboxylate clusters, molecular stand-ins for reducible metal oxide nanomaterials, mapping structure–function relationships through self-assembly and post-synthetic modification.

The school

University of Nebraska Medical Center: 20 labs on PI Pages, $657M a year on research, 82 research doctorates a year.

More about University of Nebraska Medical Center

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