Structural insights into nonheme alkylperoxoiron(III) and oxoiron(IV) intermediates by x-ray absorption spectroscopy

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dc.contributor.authorRohde, JUko
dc.contributor.authorTorelli, Sko
dc.contributor.authorShan, XPko
dc.contributor.authorLim, Mi Heeko
dc.contributor.authorKlinker, EJko
dc.contributor.authorKaizer, Jko
dc.contributor.authorChen, Kko
dc.contributor.authorNam, WWko
dc.contributor.authorQue, Lko
dc.date.accessioned2018-02-21T06:25:36Z-
dc.date.available2018-02-21T06:25:36Z-
dc.date.created2018-02-08-
dc.date.created2018-02-08-
dc.date.created2018-02-08-
dc.date.issued2004-12-
dc.identifier.citationJOURNAL OF THE AMERICAN CHEMICAL SOCIETY, v.126, no.51, pp.16750 - 16761-
dc.identifier.issn0002-7863-
dc.identifier.urihttp://hdl.handle.net/10203/240337-
dc.description.abstractTransient mononuclear low-spin alkylperoxoiron(l I I) and oxoiron(IV) complexes that are relevant to the activation of dioxygen by nonheme iron enzymes have been generated from synthetic iron(II) complexes of neutral tetradentate (TPA) and pentadentate (N4Py, Bn-TPEN) ligands and structurally characterized by means of Fe K-edge X-ray absorption spectroscopy (XAS). Notable features obtained from fits of the EXAFS region are Fe-O bond lengths of 1.78 Angstrom for the alkylperoxoiron(ill) intermediates and 1.65-1.68 Angstrom for the oxoiron(IV) intermediates, reflecting different strengths in the Fe-O pi, interactions. These differences are also observed in the intensities of the 1s-to-3d transitions in the XANES region, which increase from 4 units for the nearly octahedral iron(II) precursor to 9-15 units for the alkylperoxoiron(III) intermediates to 25-29 units for the oxoiron(IV) species.-
dc.languageEnglish-
dc.publisherAMER CHEMICAL SOC-
dc.titleStructural insights into nonheme alkylperoxoiron(III) and oxoiron(IV) intermediates by x-ray absorption spectroscopy-
dc.typeArticle-
dc.identifier.wosid000225910400032-
dc.identifier.scopusid2-s2.0-11344278017-
dc.type.rimsART-
dc.citation.volume126-
dc.citation.issue51-
dc.citation.beginningpage16750-
dc.citation.endingpage16761-
dc.citation.publicationnameJOURNAL OF THE AMERICAN CHEMICAL SOCIETY-
dc.identifier.doi10.1021/ja047667w-
dc.contributor.localauthorLim, Mi Hee-
dc.contributor.nonIdAuthorRohde, JU-
dc.contributor.nonIdAuthorTorelli, S-
dc.contributor.nonIdAuthorShan, XP-
dc.contributor.nonIdAuthorKlinker, EJ-
dc.contributor.nonIdAuthorKaizer, J-
dc.contributor.nonIdAuthorChen, K-
dc.contributor.nonIdAuthorNam, WW-
dc.contributor.nonIdAuthorQue, L-
dc.description.isOpenAccessN-
dc.type.journalArticleArticle-
dc.subject.keywordPlusTAURINE/ALPHA-KETOGLUTARATE DIOXYGENASE-
dc.subject.keywordPlusFINE-STRUCTURE SPECTROSCOPY-
dc.subject.keywordPlusPEROXIDASE COMPOUND-I-
dc.subject.keywordPlusIII-OOH INTERMEDIATE-
dc.subject.keywordPlusFE-IV=O COMPLEX-
dc.subject.keywordPlusELECTRONIC-STRUCTURE-
dc.subject.keywordPlusCRYSTAL-STRUCTURE-
dc.subject.keywordPlusSUPEROXIDE REDUCTASE-
dc.subject.keywordPlusHORSERADISH-PEROXIDASE-
dc.subject.keywordPlusOXYGEN ACTIVATION-
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