Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Mechanism of Dioxygen Activation in 2-Oxoglutarate Dependent Enzymes: A Hybrid DFT Study
Stockholm University, Faculty of Science, Department of Physics.
Stockholm University, Faculty of Science, Department of Physics.
Stockholm University, Faculty of Science, Department of Physics.
2004 (English)In: Chemistry: a European Journal, ISSN 0947-6539, Vol. 10, 1031-1041 p.Article in journal (Refereed) Published
Place, publisher, year, edition, pages
2004. Vol. 10, 1031-1041 p.
Identifiers
URN: urn:nbn:se:su:diva-22676DOI: 10.1002/chem.200305306OAI: oai:DiVA.org:su-22676DiVA: diva2:189252
Note
Part of urn:nbn:se:su:diva-103Available from: 2004-04-15 Created: 2004-04-15 Last updated: 2010-01-18Bibliographically approved
In thesis
1. Theoretical studies of mononuclear non-heme iron active sites
Open this publication in new window or tab >>Theoretical studies of mononuclear non-heme iron active sites
2004 (English)Doctoral thesis, comprehensive summary (Other academic)
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.

Place, publisher, year, edition, pages
Stockholm: Fysikum, 2004. 86 p.
Keyword
quantum chemistry, enzyme catalysis, iron enzymes
National Category
Theoretical Chemistry
Identifiers
urn:nbn:se:su:diva-103 (URN)91-7265-857-6 (ISBN)
Public defence
2004-05-07, sal FA32, AlbaNova universitetscentrum, Roslagstullsbacken 21, Stockholm, 10:00
Opponent
Supervisors
Available from: 2004-04-15 Created: 2004-04-15Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full text

Search in DiVA

By author/editor
Siegbahn, Per E. M.
By organisation
Department of Physics

Search outside of DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetric score

doi
urn-nbn
Total: 98 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf