Title

Characterization and Creation of Rubrerythrin and Symerythrin Model Proteins

Author

Katherine A. Bell, Ursinus CollegeFollow

Submission Date

7-24-2015

Document Type

Paper- Restricted to Campus Access

Department

Biochemistry & Molecular Biology

Faculty Mentor

Amanda Reig

Comments

Presented during the 17th Annual Summer Fellows Symposium, July 24, 2015 at Ursinus College.

Supported by a National Institutes of Health Academic Research Enhancement Award (AREA) grant (R15-GM110657).

Project Description

The overall goal of our research is to understand the importance of the effect of active site composition on the function of diiron proteins. Through the use of the de novo design, we have produced model proteins that mimic the active sites of rubrerythrin and symerythrin. The proteins contain one or two additional carboxylate residues, either aspartate or glutamate, at the fourteenth and forty-seventh positions. We have purified and reconstituted the proteins. The reactivity of the enzymes with oxygen and hydrogen peroxide were investigated through various assays. Our results show that both model proteins bind metal ions in a 2:1 ratio. The study of these model proteins will help us understand how structural changes in proteins can affect reactivity.

Recommended Citation

Bell, Katherine A., "Characterization and Creation of Rubrerythrin and Symerythrin Model Proteins" (2015). Biochemistry and Molecular Biology Summer Fellows. 1.
https://digitalcommons.ursinus.edu/biochem_sum/1