%0 Journal Article
%A Carboni, Michaël
%A Clémancey, Martin
%A Molton, Florian
%A Pécaut, Jacques
%A Lebrun, Colette
%A Dubois, Lionel
%A Blondin, Geneviève
%A Latour, J.-M.
%D 2012
%T Biologically Relevant
Heterodinuclear Iron–Manganese
Complexes
%U https://acs.figshare.com/articles/journal_contribution/Biologically_Relevant_Heterodinuclear_Iron_Manganese_Complexes/2482504
%R 10.1021/ic301725z.s001
%2 https://ndownloader.figshare.com/files/4125277
%K FeIIMnII
%K enzyme
%K EPR
%K susceptibility
%K FeIIIMnII
%K 1 H NMR spectroscopies
%K antiferromagnetic interaction
%K investigation
%K FeII
%K Mo
%K quasireversible electron transfer
%K cm
%K FeIII
%K analysis
%X The heterodinuclear complexes [FeIIIMnII(L-Bn)(μ-OAc)2](ClO4)2 (1) and [FeIIMnII(L-Bn)(μ-OAc)2](ClO4) (2) with the unsymmetrical
dinucleating ligand HL-Bn
{[2-bis[(2-pyridylmethyl)aminomethyl]]-6-[benzyl-2-(pyridylmethyl)aminomethyl]-4-methylphenol}
were synthesized and characterized as biologically relevant models
of the new Fe/Mn class of nonheme enzymes. Crystallographic studies
have been completed on compound 1 and reveal an FeIIIMnIIμ-phenoxobis(μ-carboxylato) core.
A single location of the FeIII ion in 1 and
of the FeII ion in 2 was demonstrated by Mössbauer
and 1H NMR spectroscopies, respectively. An investigation
of the temperature dependence of the magnetic susceptibility of 1 revealed a moderate antiferromagnetic interaction (J = 20 cm–1) between the high-spin FeIII and MnII ions in 1, which was confirmed
by Mössbauer and electron paramagnetic resonance (EPR) studies.
The electrochemical properties of complex 1 are described.
A quasireversible electron transfer at −40 mV versus Ag/AgCl
corresponding to the FeIIIMnII/FeIIMnII couple appears in the cyclic voltammogram. Thorough
investigations of the Mössbauer and EPR signatures of complex 2 were performed. The analysis allowed evidencing of a weak
antiferromagnetic interaction (J = 5.72 cm–1) within the FeIIMnII pair consistent with
that deduced from magnetic susceptibility measurements (J = 6.8 cm–1). Owing to the similar value of the
FeII zero-field splitting (DFe = 3.55 cm–1), the usual treatment within the strong
exchange limit was precluded and a full analysis of the electronic
structure of the ground state of complex 2 was developed.
This situation is reminiscent of that found in many diiron and iron–manganese
enzyme active sites.
%I ACS Publications