Submission Date

7-17-2025

Document Type

Paper- Restricted to Campus Access

Department

Chemistry

Faculty Mentor

Amanda Reig

Comments

Presented during the 27th Annual Summer Fellows Symposium, July 18, 2025 at Ursinus College.

Project Description

Metalloproteins are proteins that contain metals, often having catalytic activity. A metallohydrolase is a type of enzyme that can cleave chemical bonds using water and is responsible for important biological functions such as metabolism and detoxification. Synthetic model proteins in the Due Ferri single chain (DFsc) family were used to better understand the relationship between structure function of metallohydrolases. Originally designed to study diiron proteins, DFsc proteins can bind many 2+ transition metal ions and maintain hydrolytic abilities. Here, the catalytic activity of Zn2+-, Mn2+-, and Co2+-bound proteins were monitored using varying concentrations of bis-(4-nitrophenyl) phosphate (BNPP), which produces a product molecule that absorbs light around 405 nm when its phosphate bond is cleaved. The effects of different active-site mutations were studied by comparing the rates of G4, 3-His, 4-His, and DY DFsc proteins. Understanding the hydrolytic activity of DFsc family proteins will help explain natural metallohydrolase reactivity and aid in the production of new metallohydrolases that may be useful for the biotechnology as well as pharmaceutical fields.

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