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- W2024296976 abstract "DFsc is a single chain de novo designed four-helix bundle peptide that mimics the core protein fold and primary ligand set of various binuclear non-heme iron enzymes. DFsc and the E11D, Y51L, and Y18F single amino acid variants have been studied using a combination of near-IR circular dichroism (CD), magnetic circular dichroism (MCD), variable temperature variable field MCD (VTVH MCD), and X-ray absorption (XAS) spectroscopies. The biferrous sites are all weakly antiferromagnetically coupled with μ-1,3 carboxylate bridges and one 4-coordinate and one 5-coordinate Fe, very similar to the active site of class I ribonucleotide reductase (R2) providing open coordination positions on both irons for dioxygen to bridge. From perturbations of the MCD and VTVH MCD the iron proximal to Y51 can be assigned as the 4-coordinate center, and XAS results show that Y51 is not bound to this iron in the reduced state. The two open coordination positions on one iron in the biferrous state would become occupied by dioxygen and Y51 along the O2 reaction coordinate. Subsequent binding of Y51 functions as an internal spectral probe of the O2 reaction and as a proton source that would promote loss of H2O2. Coordination by a ligand that functions as a proton source could be a structural mechanism used by natural binuclear iron enzymes to drive their reactions past peroxo biferric level intermediates." @default.
- W2024296976 created "2016-06-24" @default.
- W2024296976 creator A5014518485 @default.
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- W2024296976 date "2008-12-17" @default.
- W2024296976 modified "2023-10-16" @default.
- W2024296976 title "Spectroscopic Definition of the Biferrous and Biferric Sites in <i>de Novo</i> Designed Four-Helix Bundle DFsc Peptides: Implications for O<sub>2</sub> Reactivity of Binuclear Non-Heme Iron Enzymes" @default.
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- W2024296976 doi "https://doi.org/10.1021/bi8016087" @default.
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