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A Density Functional Study of O-O Bond Cleavage for a Biomimetic Non-Heme Iron Complex Demonstrating an Fe(V)-Intermediate
Stockholms universitet, Naturvetenskapliga fakulteten, Fysikum.
Stockholms universitet, Naturvetenskapliga fakulteten, Fysikum.
Stockholms universitet, Naturvetenskapliga fakulteten, Fysikum.
2002 (engelsk)Inngår i: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 124, nr 37, s. 11056-11063Artikkel i tidsskrift (Fagfellevurdert) Published
sted, utgiver, år, opplag, sider
2002. Vol. 124, nr 37, s. 11056-11063
Identifikatorer
URN: urn:nbn:se:su:diva-22678DOI: 10.1021/ja026488gOAI: oai:DiVA.org:su-22678DiVA, id: diva2:189254
Merknad
Part of urn:nbn:se:su:diva-103Tilgjengelig fra: 2004-04-15 Laget: 2004-04-15 Sist oppdatert: 2017-12-13bibliografisk kontrollert
Inngår i avhandling
1. Theoretical studies of mononuclear non-heme iron active sites
Åpne denne publikasjonen i ny fane eller vindu >>Theoretical studies of mononuclear non-heme iron active sites
2004 (engelsk)Doktoravhandling, med artikler (Annet vitenskapelig)
Abstract [en]

The quantum chemical investigations presented in this thesis use hybrid density functional theory to shed light on the catalytic mechanisms of mononuclear non-heme iron oxygenases, accommodating a ferrous ion in their active sites. More specifically, the dioxygen activation process and the subsequent oxidative reactions in the following enzymes were studied: tetrahydrobiopterin-dependent hydroxylases, naphthalene 1,2-dioxygenase and α-ketoglutarate-dependent enzymes. In light of many experimental efforts devoted to the functional mimics of non-heme iron oxygenases, the reactivity of functional analogues was also examined.

The computed energetics and the available experimental data served to assess the feasibility of the reaction mechanisms investigated. Dioxygen activation in tetrahydrobiopterin- and α-ketoglutarate-dependent enzymes were found to involve a high-valent iron-oxo species, which was then capable of substrate hydroxylation. In the case of naphthalene 1,2-dioxygenase, the reactivity of an iron(III)-hydroxperoxo species toward the substrate was investigated and compared to the biomimetic counterpart.

sted, utgiver, år, opplag, sider
Stockholm: Fysikum, 2004. s. 86
Emneord
quantum chemistry, enzyme catalysis, iron enzymes
HSV kategori
Identifikatorer
urn:nbn:se:su:diva-103 (URN)91-7265-857-6 (ISBN)
Disputas
2004-05-07, sal FA32, AlbaNova universitetscentrum, Roslagstullsbacken 21, Stockholm, 10:00
Opponent
Veileder
Tilgjengelig fra: 2004-04-15 Laget: 2004-04-15bibliografisk kontrollert

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