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Laboratoire d'Electrochimie Moleculaire, LEM, Paris

UMR CNRS - Université Paris Diderot - Paris France

   
 
Master Frontiers in Chemistry | UFR de Chimie - Université Paris Diderot - Paris 7 CNRS - Institut de chimie Université de Paris Master Chimie Sorbonne Paris Cité UFR de Chimie - Université Paris Diderot - Paris 7 CNRS - Institut de chimie
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Université Paris Diderot
Université de Paris CNRS, Centre National de la Recherche Scientifique
 
 


Le LEM - Publications: Abstracts

Publication 763

Chem. Sci., 6, 639-647, 2015
DOI:10.1039/C4SC01891E
   
doi

Electrochemical study of a nonheme Fe(II) complex in the presence of dioxygen. Insights into the reductive activation of O2 at Fe(II) centers

Nathalie Ségaud, Elodie Anxolabéhère-Mallart, Katell Sénéchal-David, Laura Acosta-Rueda, Marc Robert, and Frédéric Banse

Institut de Chimie Moléculaire et des Matériaux d'Orsay, UMR CNRS 8182, Université Paris Sud, F-91405 Orsay Cedex, France
Laboratoire d'Electrochimie Moléculaire, Université Paris Diderot, Sorbonne Paris Cité, UMR 7591 CNRS, 75205 Paris Cedex 13, France

Recent efforts to model the reactivity of iron oxygenases have led to the generation of nonheme FeIII(OOH) and FeIV(O) intermediates from FeII complexes and O2 but using different cofactors. This diversity emphasizes the rich chemistry of nonheme Fe(II) complexes with dioxygen. We report an original mechanistic study of the reaction of [(TPEN)FeII]2+ with O2 carried out by cyclic voltammetry. From this FeII precursor, reaction intermediates such as [(TPEN)FeIV(O)]2+, [(TPEN)FeIII(OOH)]2+ and [(TPEN)FeIII(OO)]+ have been chemically generated in high yield, and characterized electrochemically. These electrochemical data have been used to analyse and perform simulation of the cyclic voltammograms of [(TPEN)FeII]2+ in the presence of O2. Thus, several important mechanistic informations on this reaction have been obtained. An unfavourable chemical equilibrium between O2 and the FeII complex occurs that leads to the FeIII-peroxo complex upon reduction, similarly to heme enzymes such as P450. However, unlike in heme systems, further reduction of this latter intermediate does not result in OľO bond cleavage.

 
   
 
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