Submission Date


Document Type

Paper- Restricted to Campus Access


Biochemistry & Molecular Biology


Amanda Reig

Committee Member

Samantha Wilner

Committee Member

Hugo Montesinos-Yufa

Department Chair

Eric Williamsen

Department Chair

Anthony Lobo

Project Description

Metalloproteins are found in nature and involved in biological processes, especially in the cleavage of various molecular bonds. Of particular relevance are metallohydrolases, a class of enzymes that have the ability to catalyze hydrolysis by using water to break chemical bonds and using their metal cofactors to aid in this process. To better understand these natural enzymes, the de novo designed non-heme four-helix bundle Due Ferri single chain (DFsc) protein is used as a model system as it has a similar binuclear active site composition. The simpler structure of this model is helpful for studying the complex mechanism of DNA cleavage and better understand the protein’s structure-function relationship as a hydrolase. Here we investigated the ability of DFsc to cleave and linearize the pUC19 plasmid, changing different parameters, like metal cofactors and protein active site composition.


This project was funded by the National Institutes of Health (NIH grant R15-GM144906-01).