Diiron(II) μ-aqua-μ-hydroxo model for non-heme iron sites in proteins

Ivan V. Korendovych; Sergey V. Kryatov; William M. Reiff; Elena V. Rybak-Akimova

doi:10.1021/ic051739i

Diiron(II) μ-aqua-μ-hydroxo model for non-heme iron sites in proteins

Ivan V. Korendovych, Sergey V. Kryatov, William M. Reiff, Elena V. Rybak-Akimova

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21 Scopus citations

Abstract

We have synthesized a diiron(II) complex with a novel aquahydroxo 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.

Original language	English (US)
Pages (from-to)	8656-8658
Number of pages	3
Journal	Inorganic Chemistry
Volume	44
Issue number	24
DOIs	https://doi.org/10.1021/ic051739i
State	Published - Nov 28 2005
Externally published	Yes

ASJC Scopus subject areas

Physical and Theoretical Chemistry
Inorganic Chemistry

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10.1021/ic051739i

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title = "Diiron(II) μ-aqua-μ-hydroxo model for non-heme iron sites in proteins",

abstract = "We have synthesized a diiron(II) complex with a novel aquahydroxo 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.",

author = "Korendovych, {Ivan V.} and Kryatov, {Sergey V.} and Reiff, {William M.} and Rybak-Akimova, {Elena V.}",

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T1 - Diiron(II) μ-aqua-μ-hydroxo model for non-heme iron sites in proteins

AU - Korendovych, Ivan V.

AU - Kryatov, Sergey V.

AU - Reiff, William M.

AU - Rybak-Akimova, Elena V.

PY - 2005/11/28

Y1 - 2005/11/28

N2 - We have synthesized a diiron(II) complex with a novel aquahydroxo 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.

AB - We have synthesized a diiron(II) complex with a novel aquahydroxo 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.

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Diiron(II) μ-aqua-μ-hydroxo model for non-heme iron sites in proteins

Abstract

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