Spectroscopy and electronic structures of mono- and binuclear high-valent non-heme iron-oxo systems.
J Inorg Biochem
; 100(4): 697-706, 2006 Apr.
Article
em En
| MEDLINE
| ID: mdl-16510189
ABSTRACT
High-valent iron-oxo intermediates are known or believed to be key oxidizing species in the catalytic mechanisms of many mononuclear and binuclear non-heme iron enzymes. So far only limited experimental data on their electronic structures are available. In this study we extend knowledge from the experimentally well characterized mononuclear Fe(IV)=O (S=1) biomimetic model system to computational insight into the spectroscopy and electronic structures of mono-and binuclear high-valent iron-oxo enzyme intermediates. In the mononuclear Fe(IV)=O complexes, we predict the spectroscopy and energies of the electronic transitions to be very different for the S=1 and S=2 spin states, but the iron-oxo bonding for both spin states to be very similar. A comparison of the S=2 mono- and binuclear high-valent iron-sites predicts similar electronic transitions. However, the bent iron-oxo bridge and interactions with the second iron-center in the dimer shift the transitions to higher energies and splits the d(xz/yz) orbital set. These electronic structure and TD-DFT results provide a basis for understanding the spectroscopy and electronic structures of high-valent intermediates in mono- and binuclear non-heme iron enzymes.
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Base de dados:
MEDLINE
Assunto principal:
Oxigênio
/
Ferroproteínas não Heme
/
Materiais Biomiméticos
/
Ferro
Tipo de estudo:
Prognostic_studies
Idioma:
En
Ano de publicação:
2006
Tipo de documento:
Article