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

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dc.contributor.authorSolomon, Edward I.ko
dc.contributor.authorPark, Kiyoungko
dc.date.accessioned2016-11-09T02:38:28Z-
dc.date.available2016-11-09T02:38:28Z-
dc.date.created2016-10-05-
dc.date.created2016-10-05-
dc.date.issued2016-09-
dc.identifier.citationJOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, v.21, no.5-6, pp.575 - 588-
dc.identifier.issn0949-8257-
dc.identifier.urihttp://hdl.handle.net/10203/213510-
dc.description.abstractBinuclear 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-
dc.languageEnglish-
dc.publisherSPRINGER-
dc.subjectMAGNETIC CIRCULAR-DICHROISM-
dc.subjectCOLI RIBONUCLEOTIDE REDUCTASE-
dc.subjectMETHANE MONOOXYGENASE HYDROXYLASE-
dc.subjectACYL CARRIER PROTEIN-
dc.subjectMETHYLOSINUS-TRICHOSPORIUM OB3B-
dc.subjectELECTRONIC-STRUCTURE CONTRIBUTIONS-
dc.subjectMETHYLOCOCCUS-CAPSULATUS BATH-
dc.subjectREVERSIBLE DIOXYGEN BINDING-
dc.subjectN-OXYGENASE AURF-
dc.subjectMYOINOSITOL OXYGENASE-
dc.titleStructure/function correlations over binuclear non-heme iron active sites-
dc.typeArticle-
dc.identifier.wosid000382127000002-
dc.identifier.scopusid2-s2.0-84976520613-
dc.type.rimsART-
dc.citation.volume21-
dc.citation.issue5-6-
dc.citation.beginningpage575-
dc.citation.endingpage588-
dc.citation.publicationnameJOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY-
dc.identifier.doi10.1007/s00775-016-1372-9-
dc.contributor.localauthorPark, Kiyoung-
dc.contributor.nonIdAuthorSolomon, Edward I.-
dc.type.journalArticleReview-
dc.subject.keywordAuthorBinuclear non-heme iron enzymes-
dc.subject.keywordAuthorO-2 activation-
dc.subject.keywordAuthorVariable-temperature-
dc.subject.keywordAuthorvariable-field magnetic circular dichroism-
dc.subject.keywordAuthorFrontier molecular orbitals-
dc.subject.keywordAuthorPeroxide activation-
dc.subject.keywordPlusMAGNETIC CIRCULAR-DICHROISM-
dc.subject.keywordPlusCOLI RIBONUCLEOTIDE REDUCTASE-
dc.subject.keywordPlusMETHANE MONOOXYGENASE HYDROXYLASE-
dc.subject.keywordPlusACYL CARRIER PROTEIN-
dc.subject.keywordPlusMETHYLOSINUS-TRICHOSPORIUM OB3B-
dc.subject.keywordPlusELECTRONIC-STRUCTURE CONTRIBUTIONS-
dc.subject.keywordPlusMETHYLOCOCCUS-CAPSULATUS BATH-
dc.subject.keywordPlusREVERSIBLE DIOXYGEN BINDING-
dc.subject.keywordPlusN-OXYGENASE AURF-
dc.subject.keywordPlusMYOINOSITOL OXYGENASE-
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