Matches in SemOpenAlex for { <https://semopenalex.org/work/W2465783544> ?p ?o ?g. }
- W2465783544 endingPage "588" @default.
- W2465783544 startingPage "575" @default.
- W2465783544 abstract "Binuclear non-heme iron enzymes activate O2 to perform diverse chemistries. Three different structural mechanisms of O2 binding to a coupled binuclear iron site have been identified utilizing variable-temperature, variable-field magnetic circular dichroism spectroscopy (VTVH MCD). For the μ-OH-bridged Fe(II)2 site in hemerythrin, O2 binds terminally to a five-coordinate Fe(II) center as hydroperoxide with the proton deriving from the μ-OH bridge and the second electron transferring through the resulting μ-oxo superexchange pathway from the second coordinatively saturated Fe(II) center in a proton-coupled electron transfer process. For carboxylate-only-bridged Fe(II)2 sites, O2 binding as a bridged peroxide requires both Fe(II) centers to be coordinatively unsaturated and has good frontier orbital overlap with the two orthogonal O2 π* orbitals to form peroxo-bridged Fe(III)2 intermediates. Alternatively, carboxylate-only-bridged Fe(II)2 sites with only a single open coordination position on an Fe(II) enable the one-electron formation of Fe(III)–O2 − or Fe(III)–NO− species. Finally, for the peroxo-bridged Fe(III)2 intermediates, further activation is necessary for their reactivities in one-electron reduction and electrophilic aromatic substitution, and a strategy consistent with existing spectral data is discussed." @default.
- W2465783544 created "2016-07-22" @default.
- W2465783544 creator A5024342453 @default.
- W2465783544 creator A5048407979 @default.
- W2465783544 date "2016-07-01" @default.
- W2465783544 modified "2023-09-27" @default.
- W2465783544 title "Structure/function correlations over binuclear non-heme iron active sites" @default.
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