Linked Life Data

16241166

Source:http://linkedlifedata.com/resource/pubmed/id/16241166

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
22
pubmed:dateCreated
2005-10-24
pubmed:abstractText
Oxidizing intermediates are generated from nonheme iron(III) complexes to investigate the electronic structure and the reactivity, in comparison with the oxoiron(IV) porphyrin pi-cation radical (compound I) as a heme enzyme model. Sterically hindered iron salen complexes, bearing a fifth ligand Cl (1), OH(2) (2), OEt (3), and OH (4), are oxidized both electrochemically and chemically. Stepwise one-electron oxidation of 1 and 2 generates iron(III)-mono- and diphenoxyl radicals, as revealed by detailed spectroscopic investigations, including UV-vis, EPR, Mössbauer, resonance Raman, and ESIMS spectroscopies. In contrast to the oxoiron(IV) formation from the hydroxoiron(III) porphyrin upon one-electron oxidation, the hydroxo complex 4 does not generate oxoiron(IV) species. Reaction of 2 with mCPBA also results in the formation of the iron(III)-phenoxyl radical. One-electron oxidation of 3 leads to oxidative degradation of the fifth EtO ligand to liberate acetaldehyde even at 203 K. The iron(III)-phenoxyl radical shows high reactivity for alcoxide on iron(III) but exhibits virtually no reactivity for alcohols including even benzyl alcohol without a base to remove an alcohol proton. This study explains unique properties of mononuclear nonheme enzymes with Tyr residues and also the poor epoxidation activity of Fe salen compared to Mn and Cr salen compounds.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0020-1669
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8156-66
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Oxidizing intermediates from the sterically hindered iron salen complexes related to the oxygen activation by nonheme iron enzymes.
pubmed:affiliation
Institute for Molecular Science & Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, Myodaiji, Aichi, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't