Rupal Gupta
College of Staten Island CUNY, NY·Biochemistry
Metal ions sit at the heart of many proteins and decide what those proteins can do. Two questions run through this research.
- Fields
Biochemistry
Chemistry
Biophysics
- Topics
non-heme iron enzymes
metalloenzymes
3-His motif
- Grants
- 2 known grants, through Aug 2027
What they work on
- Determine how 3-His iron-binding sites, an unusual alternative to the common 2-His-1-carboxylate motif, change the reaction mechanisms of non-heme iron enzymes that cut aromatic rings, using biochemical and spectroscopic methods.
- Measure reaction kinetics and the electronic and magnetic properties of reaction intermediates in 3-His ring-cleaving enzymes to show how the metal's immediate surroundings control reactivity and substrate selectivity.
- Test how calcium binding regulates the structure, flexibility and functions of S100A12, an immune protein that starves microbes of zinc, using biophysical methods in vitro.
- Examine how calcium and zinc binding drive S100A12 signaling and its interaction with membrane receptors such as RAGE, testing the idea that metal binding links its antimicrobial and pro-inflammatory roles.
More about the research
How does the exact way a metal is held inside a protein change the chemistry it performs? And how does binding of metals such as zinc and calcium switch a protein between different jobs? One project studies iron enzymes that break apart ring-shaped aromatic molecules. The other studies S100A12, a human immune protein that both starves microbes of metals and triggers inflammation.
Why it matters
Understanding how the immune protein S100A12 connects metal capture to inflammation could help in developing therapies that target such molecules during harmful, excessive inflammation, and in inhibiting microbial infection. Findings on how unusual iron-binding sites control enzyme reactions could guide the design of artificial catalysts for difficult chemical reactions, such as breaking aromatic rings.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
The Influence of Primary Coordination Sphere in Aromatic C-C Ring Scission: Mechanistic Studies of 3-His Coordinated Non-heme Iron Enzymes
NSF · Sep 2021 – Aug 2027
Interdependence of Antimicrobial and Pro-inflammatory Activities Mediated by S100A12 in the Innate Immune Response
NIH · Aug 2019 – Aug 2026
Closest labs
Gayan Wijeratne
University of Alabama, AL·Chemistry
Synthesize heme-nitrogen oxide model complexes with systematically varied ligands in the primary and secondary coordination spheres, to find which features of the heme center control the geometry and electronic structure of these intermediates.
Joseph M Bollinger
Pennsylvania State University, PA·Biochemistry
Determine how iron(II) and 2-oxoglutarate-dependent (Fe/2OG) oxygenases direct a common oxoiron(IV) intermediate toward hydroxylation, halogenation, desaturation, or cyclization, and test this by rationally redirecting reaction outcomes.
John Gilbertson
Western Washington University, WA·Chemistry
Develop a class of ditopic receptors, metal complexes with two hydrogen-bond-donating sites near the metal, that capture and reduce nitrite and nitrate (NOx-), built on the redox-active pyridinediimine (PDI) ligand.
The school
College of Staten Island CUNY: 2 labs on PI Pages, $6M a year on research, 3 research doctorates a year.
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