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Titolo:
O-2 activation by nonheme iron complexes: A monomeric Fe(III)-oxo complex derived from O-2
Autore:
MacBeth, CE; Golombek, AP; Young, VG; Yang, C; Kuczera, K; Hendrich, MP; Borovik, AS;
Indirizzi:
Univ Kansas, Dept Chem, Lawrence, KS 66045 USA Univ Kansas Lawrence KS USA 66045 nsas, Dept Chem, Lawrence, KS 66045 USA Univ Kansas, Dept Mol Biosci, Lawrence, KS 66045 USA Univ Kansas LawrenceKS USA 66045 Dept Mol Biosci, Lawrence, KS 66045 USA Carnegie Mellon Univ, Dept Chem, Pittsburgh, PA 15213 USA Carnegie Mellon Univ Pittsburgh PA USA 15213 em, Pittsburgh, PA 15213 USA Univ Minnesota, Dept Chem, Minneapolis, MN 55455 USA Univ Minnesota Minneapolis MN USA 55455 t Chem, Minneapolis, MN 55455 USA
Titolo Testata:
SCIENCE
fascicolo: 5481, volume: 289, anno: 2000,
pagine: 938 - 941
SICI:
0036-8075(20000811)289:5481<938:OABNIC>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
BOND-DISSOCIATION ENERGIES; HEME-CONTAINING OXYGENASES; HORSERADISH-PEROXIDASE; EXAFS SPECTROSCOPY; COMPOUND-I; OXO; MANGANESE(III); RECOGNITION; HEMOGLOBIN; MECHANISMS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Borovik, AS Univ Kansas, Dept Chem, Lawrence, KS 66045 USA Univ Kansas Lawrence KS USA 66045 hem, Lawrence, KS 66045 USA
Citazione:
C.E. MacBeth et al., "O-2 activation by nonheme iron complexes: A monomeric Fe(III)-oxo complex derived from O-2", SCIENCE, 289(5481), 2000, pp. 938-941

Abstract

Iron species with terminal oxo Ligands are implicated as key intermediatesin several synthetic and biochemical catalytic cycles. However, there is adearth of structural information regarding these types of complexes because their instability has precluded isolation under ambient conditions. The isolation and structural characterization of an iron(III) complex with a terminal oxo Ligand, derived directly from dioxygen (O-2), is reported. A stable structure resulted from placing the oxoiron unit within a synthetic cavity Lined with hydrogen-bonding groups. The cavity creates a microenvironment around the iron center that aids in regulating O-2 activation and stabilizing the oxoiron unit. These cavities share properties with the active sites of metalloproteins, where function is correlated strongly with site structure.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/09/20 alle ore 18:42:21