Diiron(II) μ-Aqua-μ-hydroxo Model for Non-Heme Iron Sites in Proteins

We have synthesized a diiron(II) complex with a novel aqua−hydroxo bridging motif, [Fe2(μ-H2O)(μ-OH)(TPA)2](OTf)3 (1). This is a new member of the diiron diamond core family. The complex is stable in solution in nonpolar solvents as well as in the solid state. Two high-spin iron(II) sites are antife...

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Bibliographic Details
Published in:Inorganic chemistry 2005-11, Vol.44 (24), p.8656-8658
Main Authors: Korendovych, Ivan V, Kryatov, Sergey V, Reiff, William M, Rybak-Akimova, Elena V
Format: Article
Language:English
Subjects:
Binding Sites
Chemistry, Inorganic - methods
Electrochemistry - methods
Electron Transport
Ferrous Compounds - chemistry
Ferrous Compounds - metabolism
Heme - chemistry
Heme - metabolism
Iron - metabolism
Ligands
Models, Molecular
Molecular Conformation
Molecular Structure
Oxygen - chemistry
Proteins - chemistry
Proteins - metabolism
Spectrometry, Mass, Electrospray Ionization - methods
Spectrophotometry, Ultraviolet
Temperature
Water
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Summary:We have synthesized a diiron(II) complex with a novel aqua−hydroxo bridging motif, [Fe2(μ-H2O)(μ-OH)(TPA)2](OTf)3 (1). This is a new member of the diiron diamond core family. The complex is stable in solution in nonpolar solvents as well as in the solid state. Two high-spin iron(II) sites are antiferromagnetically coupled (J = −9.6 cm-1). The drastic difference of ca. 1 V in the redox potential between complex 1 and its bis(hydroxo)-bridged analogue Fe2(OH)2(TPA)3+ is accompanied by only a moderate difference in the dioxygen reactivity. This observation is consistent with the inner-sphere mechanism of iron(II)−dioxygen association rather than the outer-sphere electron transfer.
ISSN:0020-1669
1520-510X
DOI:10.1021/ic051739i