Submission Date

7-24-2020

Document Type

Paper- Restricted to Campus Access

Department

Chemistry

Faculty Mentor

Amanda Reig

Comments

Presented during the 22nd Annual Summer Fellows Symposium, July 24, 2020 at Ursinus College.

This material is based upon work supported by the National Science Foundation under Grant No. 1458719. Any opinions, findings, and conclusions or recommendations expressed in this material are those of the author(s) and do not necessarily reflect the views of the National Science Foundation.

A related presentation is available here.

Project Description

Many proteins that are found in nature and involved in biological processes have metal ions bound at their core. Iron is commonly used by proteins because of its high bioavailability and redox properties, which make it well suited for many reactions. Of particular relevance are diiron carboxylate enzymes, a class of proteins that are structurally similar but carry out a wide range of biologically important reactions. To better understand the factors that affect how efficiently these reactions occur, we use the de novo designed Due Ferri single chain (DFsc) protein as a model system. DFsc mimics the active site structure of diiron carboxylate enzymes within a minimalist protein fold. In this work, we use cyclic voltammetry to investigate the electrochemical properties of the DFsc model and its variants to quantify the electron transfer and redox activity. Learning more about the redox properties of the DFsc model can provide a clearer understanding of how and why diiron carboxylate proteins carry out their specific chemical reactions.

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