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Biochemistry & Molecular Biology
G4Dfsc is a de novo designed, single-chain four-helix bundle protein created to mimic the properties of diiron carboxylate enzymes. The active sites of these proteins are comprised of two iron atoms ligated by two histidine and four carboxylate residues. One similar binuclear non-heme enzyme is flavin-dependent nitric oxide reductase (FprA), which contains a 4-His/3-carboyxlate iron-binding motif. This particular protein initiates the reduction of NO to N2O and H2O. To create a model protein that mimics this chemistry, two G4Dfsc variants with 4-His/3-carboyxlate active sites have been created. Structural analysis of these mutated proteins provides molecular-level insights into their differences and provides a better understanding of the influence of each active site amino acid residue. By understanding the roles of these amino acids, it will ultimately provide an understanding of the stability and reactivity of natural binuclear non-heme iron enzymes.
O'Shea, Katherine, "Structural and Functional Characterization of 3HisG4Dfsc" (2015). Biochemistry and Molecular Biology Summer Fellows. 2.
Available to Ursinus community only.
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).
Supported also by a Howard Hughes Medical Institute (HHMI) grant.