Theoretical Exploration of the Oxidative Properties of a [(trenMe1)CuO2]+ Adduct Relevant to Copper Monooxygenase Enzymes: Insights into Competitive Dehydrogenation versus Hydroxylation Reaction Pathways
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Mostrar el registro completo del ítemcomunitat-uji-handle:10234/9
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http://dx.doi.org/10.1002/chem.200701595 |
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Título
Theoretical Exploration of the Oxidative Properties of a [(trenMe1)CuO2]+ Adduct Relevant to Copper Monooxygenase Enzymes: Insights into Competitive Dehydrogenation versus Hydroxylation Reaction PathwaysFecha de publicación
2008-07Editor
WileyISSN
0947-6539Cita bibliográfica
Chemistry - A European Journal, 14, 21, p. 6465–6473Tipo de documento
info:eu-repo/semantics/articleVersión de la editorial
http://onlinelibrary.wiley.com/doi/10.1002/chem.200701595/fullVersión
info:eu-repo/semantics/publishedVersionPalabras clave / Materias
Resumen
Singlet and triplet H-transfer reaction paths from CH and NH bonds were examined by means of DFT and spin-flip TD-DFT computations on the [(trenMe1)CuO2]+ adduct. The singlet energy surfaces allow its evolution towards ... [+]
Singlet and triplet H-transfer reaction paths from CH and NH bonds were examined by means of DFT and spin-flip TD-DFT computations on the [(trenMe1)CuO2]+ adduct. The singlet energy surfaces allow its evolution towards H2O2 and an imine species. Whereas NH cleavage appears to be a radical process, CH rupture results in a carbocation intermediate stabilized by an adjacent N atom and an electrostatic interaction with the [CuIOOH] metal core. Upon injection of an additional electron, the latter species straightforwardly forms a hydroxylated product. Based on these computational results, a new mechanistic description of the reactivity of copper monooxygenases is proposed. [-]
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Copyright © 2008 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
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