DC Field | Value | Language |
---|---|---|
dc.contributor.author | Solomon, Edward I. | ko |
dc.contributor.author | Park, Kiyoung | ko |
dc.date.accessioned | 2016-11-09T02:38:28Z | - |
dc.date.available | 2016-11-09T02:38:28Z | - |
dc.date.created | 2016-10-05 | - |
dc.date.created | 2016-10-05 | - |
dc.date.issued | 2016-09 | - |
dc.identifier.citation | JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, v.21, no.5-6, pp.575 - 588 | - |
dc.identifier.issn | 0949-8257 | - |
dc.identifier.uri | http://hdl.handle.net/10203/213510 | - |
dc.description.abstract | 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 | - |
dc.language | English | - |
dc.publisher | SPRINGER | - |
dc.subject | MAGNETIC CIRCULAR-DICHROISM | - |
dc.subject | COLI RIBONUCLEOTIDE REDUCTASE | - |
dc.subject | METHANE MONOOXYGENASE HYDROXYLASE | - |
dc.subject | ACYL CARRIER PROTEIN | - |
dc.subject | METHYLOSINUS-TRICHOSPORIUM OB3B | - |
dc.subject | ELECTRONIC-STRUCTURE CONTRIBUTIONS | - |
dc.subject | METHYLOCOCCUS-CAPSULATUS BATH | - |
dc.subject | REVERSIBLE DIOXYGEN BINDING | - |
dc.subject | N-OXYGENASE AURF | - |
dc.subject | MYOINOSITOL OXYGENASE | - |
dc.title | Structure/function correlations over binuclear non-heme iron active sites | - |
dc.type | Article | - |
dc.identifier.wosid | 000382127000002 | - |
dc.identifier.scopusid | 2-s2.0-84976520613 | - |
dc.type.rims | ART | - |
dc.citation.volume | 21 | - |
dc.citation.issue | 5-6 | - |
dc.citation.beginningpage | 575 | - |
dc.citation.endingpage | 588 | - |
dc.citation.publicationname | JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY | - |
dc.identifier.doi | 10.1007/s00775-016-1372-9 | - |
dc.contributor.localauthor | Park, Kiyoung | - |
dc.contributor.nonIdAuthor | Solomon, Edward I. | - |
dc.type.journalArticle | Review | - |
dc.subject.keywordAuthor | Binuclear non-heme iron enzymes | - |
dc.subject.keywordAuthor | O-2 activation | - |
dc.subject.keywordAuthor | Variable-temperature | - |
dc.subject.keywordAuthor | variable-field magnetic circular dichroism | - |
dc.subject.keywordAuthor | Frontier molecular orbitals | - |
dc.subject.keywordAuthor | Peroxide activation | - |
dc.subject.keywordPlus | MAGNETIC CIRCULAR-DICHROISM | - |
dc.subject.keywordPlus | COLI RIBONUCLEOTIDE REDUCTASE | - |
dc.subject.keywordPlus | METHANE MONOOXYGENASE HYDROXYLASE | - |
dc.subject.keywordPlus | ACYL CARRIER PROTEIN | - |
dc.subject.keywordPlus | METHYLOSINUS-TRICHOSPORIUM OB3B | - |
dc.subject.keywordPlus | ELECTRONIC-STRUCTURE CONTRIBUTIONS | - |
dc.subject.keywordPlus | METHYLOCOCCUS-CAPSULATUS BATH | - |
dc.subject.keywordPlus | REVERSIBLE DIOXYGEN BINDING | - |
dc.subject.keywordPlus | N-OXYGENASE AURF | - |
dc.subject.keywordPlus | MYOINOSITOL OXYGENASE | - |
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