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Theoretical study of the hydroxylation of phenols mediated by an end-on bound superoxo-copper(II) complex
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Physics.
2009 (English)In: Journal of Biological Inorganic Chemistry, ISSN 0949-8257, E-ISSN 1432-1327, Vol. 14, no 2, 273-285 p.Article in journal (Refereed) Published
Abstract [en]

Peptidylglycine alpha-amidating monooxygenase and dopamine beta-monooxygenase are copper-containing proteins which catalyze essential hydroxylation reactions in biological systems. There are several possible mechanisms for the reductive O-2-activation at their mononuclear copper active site. Recently, Karlin and coworkers reported on the reactivity of a copper(II)-superoxo complex which is capable of inducing the hydroxylation of phenols with incorporated oxygen atoms derived from the Cu(II)-O-2(-) moiety. In the present work the reaction mechanism for the abovementioned superoxo complex with phenols is studied. The pathways found are analyzed with the aim of providing some insight into the nature of the chemical and biological copper-promoted oxidative processes with 1:1 Cu(I)/O-2-derived species.

Place, publisher, year, edition, pages
2009. Vol. 14, no 2, 273-285 p.
Keyword [en]
Copper enzymes, Mononuclear copper complexes, Hydroxylation of phenols, Density functional theory, B3LYP functional
National Category
Physical Sciences
Identifiers
URN: urn:nbn:se:su:diva-60244DOI: 10.1007/s00775-008-0447-7ISI: 000264102000012OAI: oai:DiVA.org:su-60244DiVA: diva2:434160
Note
authorCount :4Available from: 2011-08-12 Created: 2011-08-11 Last updated: 2017-12-08Bibliographically approved

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Siegbahn, Per E. M.
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