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Ascorbate Peroxidase Compound II Is an Iron(IV) Oxo Species

Ledray, Aaron P ; Krest, Courtney M ; Yosca, Timothy H ; Mittra, Kaustuv ; Green, Michael T

Journal of the American Chemical Society, 2020-12, Vol.142 (48), p.20419-20425 [Periódico revisado por pares]

United States: American Chemical Society

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  • Título:
    Ascorbate Peroxidase Compound II Is an Iron(IV) Oxo Species
  • Autor: Ledray, Aaron P ; Krest, Courtney M ; Yosca, Timothy H ; Mittra, Kaustuv ; Green, Michael T
  • É parte de: Journal of the American Chemical Society, 2020-12, Vol.142 (48), p.20419-20425
  • Notas: ObjectType-Article-1
    SourceType-Scholarly Journals-1
    ObjectType-Feature-2
    content type line 23
  • Descrição: The protonation state of the iron­(IV) oxo (or ferryl) form of ascorbate peroxidase compound II (APX-II) is a subject of debate. It has been reported that this intermediate is best described as an iron­(IV) hydroxide species. Neutron diffraction data obtained from putative APX-II crystals indicate a protonated oxygenic ligand at 1.88 Å from the heme iron. This finding, if correct, would be unprecedented. A basic iron­(IV) oxo species has yet to be spectroscopically observed in a histidine-ligated heme enzyme. The importance of ferryl basicity lies in its connection to our fundamental understanding of C–H bond activation. Basic ferryl species have been proposed to facilitate the oxidation of inert C–H bonds, reactions that are unknown for histidine-ligated hemes enzymes. To provide further insight into the protonation status of APX-II, we examined the intermediate using a combination of Mössbauer and X-ray absorption spectroscopies. Our data indicate that APX-II is an iron­(IV) oxo species with an Fe–O bond distance of 1.68 Å, a K-edge pre-edge absorption of 18 units, and Mössbauer parameters of ΔE q = 1.65 mm/s and δ = 0.03 mm/s.
  • Editor: United States: American Chemical Society
  • Idioma: Inglês
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