Structure/function correlations over binuclear non-heme iron active sites

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Binuclear non-heme iron enzymes activate O-2 to perform diverse chemistries. Three different structural mechanisms of O-2 binding to a coupled binuclear iron site have been identified utilizing variable-temperature, variable-field magnetic circular dichroism spectroscopy (VTVH MCD). For the mu-OH-bridged Fe(II)(2) site in hemerythrin, O-2 binds terminally to a five-coordinate Fe(II) center as hydroperoxide with the proton deriving from the mu-OH bridge and the second electron transferring through the resulting mu-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, O-2 binding as a bridged peroxide requires both Fe(II) centers to be coordinatively unsaturated and has good frontier orbital overlap with the two orthogonal O-2 pi* 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)-O-2 (-) 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
Publisher
SPRINGER
Issue Date
2016-09
Language
English
Article Type
Review
Keywords

MAGNETIC CIRCULAR-DICHROISM; COLI RIBONUCLEOTIDE REDUCTASE; METHANE MONOOXYGENASE HYDROXYLASE; ACYL CARRIER PROTEIN; METHYLOSINUS-TRICHOSPORIUM OB3B; ELECTRONIC-STRUCTURE CONTRIBUTIONS; METHYLOCOCCUS-CAPSULATUS BATH; REVERSIBLE DIOXYGEN BINDING; N-OXYGENASE AURF; MYOINOSITOL OXYGENASE

Citation

JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, v.21, no.5-6, pp.575 - 588

ISSN
0949-8257
DOI
10.1007/s00775-016-1372-9
URI
http://hdl.handle.net/10203/213510
Appears in Collection
CH-Journal Papers(저널논문)
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