Diiron(II) complexes showing a reversible oxygenation induced by a proton transfer mediated with a water molecule. Biological implication of a water molecule in hemerythrin function

Arii, Hidekazu; Funahashi, Yasuhiro; Ozawa, Tomohiro; Jitsukawa, Koichiro; Masuda, Hideki

doi:10.1016/j.jorganchem.2006.04.052

Cited by 8 publications

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“…Suitable model compounds can provide insight into these factors. Indeed, in the past 20 years, many synthetic peroxodiferric complexes have been trapped and spectroscopically characterized from the reactions of diiron(II) precursors with O 2 or diiron(III) complexes with H 2 O 2 . ,− Some of these intermediates are stable enough to have been crystallized, and the crystal structures of five such complexes have been reported. − , In each case, there is a ( cis -μ-1,2-peroxo)diferric center that is supported by one or two additional bridging groups such as oxo, hydroxo, alkoxo, and/or a bidentate carboxylate, which constrain the Fe···Fe distances to a range from 3.2 to 4 Å (Table ). The relative stability of these peroxo intermediates has allowed their structural and spectroscopic properties to be determined and used to shed light on the nature of the corresponding enzyme intermediates.…”

Section: Introductionmentioning

confidence: 99%

Protonation of a Peroxodiiron(III) Complex and Conversion to a Diiron(III/IV) Intermediate: Implications for Proton-Assisted O–O Bond Cleavage in Nonheme Diiron Enzymes

et al. 2012

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Oxygenation of a diiron(II) complex,[FeII2(μ-OH)2(BnBQA)2(NCMe)2]2+ (2) (where BnBQA is N-benzyl-N,N-bis(2-quinolinylmethyl)amine) results in the formation of a metastable peroxodiferric intermediate (3). Treatment of 3 with strong acid affords its conjugate acid 4 in which the (μ-oxo)(μ-1,2-peroxo)diiron(III) core of 3 is protonated at the oxo bridge. The core structures of 3 and 4 are characterized in detail by UV-vis, Mössbauer, resonance Raman, and X-ray absorption spectroscopies. Complex 4 is shorter lived than 3 and decays to generate in 20–25% yield a diiron(III/IV) species (5) that can be identified by EPR and Mössbauer spectroscopy. This reaction sequence demonstrates for the first time that protonation of the oxo bridge of a (μ-oxo)(μ-1,2-peroxo)diiron(III) complex leads to the cleavage of the peroxo O–O bond and formation of a high-valent diiron complex, thereby mimicking the steps involved in the formation of intermediate X in the activation cycle of ribonucleotide reductase.

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Section: Introductionmentioning

confidence: 99%

Protonation of a Peroxodiiron(III) Complex and Conversion to a Diiron(III/IV) Intermediate: Implications for Proton-Assisted O–O Bond Cleavage in Nonheme Diiron Enzymes

et al. 2012

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“…However, almost diiron model complexes generated Oz-adduct only in non-aqueous solution at low temperature [24][25][26][27][28][29].…”

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confidence: 98%

Preparation of Au Electrodes Modified with Self-assembled Monolayers of Functional Metal Complexes

Masuda¹

2007

Trans. Mat. Res. Soc. Japan

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In this paper, we review our recent works on the preparations of some Au electrodes modified with self-assembled monolayers of functional metal complexes. such as molecular recognition, electron transfer, bacteria immobilization, and dioxygen activation, from the viewpoint of the construction of chemical/energetic conversion devices. (i) A new-classed promoter electrode bearing optically-active Com complexes containing (5)-/(R)-phenylalaninc derivative ligands as the molecular recognition site has been constructed: the chirality and/or orientation of promoter on Au electrode surface have affected the electron transfer rate of cytochrome c. (ii) The Fell1-artificial siderophore-modified Au electrode surface has been prepared as an immobilizing tool of microorganisms toward the bacteria sensor and bio-reactor, whose adsorption ability for microorganisms has been studied. (iii) For a purpose of fixation and activation of dioxygen at room temperature, the self-assembled monolayer of dinuclear iron complex has been modified on Au electrode. and its reaction with dioxygen has been studied.

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An Iron(II)[1,3‐bis(2′‐pyridylimino)isoindoline] Complex as a Catalyst for Substrate Oxidation with H₂O₂ – Evidence for a Transient Peroxidodiiron(III) Species

et al. 2013

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The complex [Fe(indH)(solvent)3](ClO4)2 (1) has been isolated from the reaction of equimolar amounts of 1,3-bis(2′-pyridylimino)isoindoline (indH) and Fe(ClO4)2 in acetonitrile and characterized by X-ray crystallography and several spectroscopic techniques. It is a suitable catalyst for the oxidation of thioanisoles and benzyl alcohols with H2O2 as the oxidant. Hammett correlations and kinetic isotope effect experiments support the involvement of an electrophilic metal-based oxidant. A metastable green species (2) is observed when 1 is reacted with H2O2 at −40 °C, which has been characterized to have a FeIII(μ-O)(μ-O2)FeIII core on the basis of UV-Vis, electron paramagnetic resonance, resonance Raman, and X-ray absorption spectroscopic data.

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Diiron(II) complexes showing a reversible oxygenation induced by a proton transfer mediated with a water molecule. Biological implication of a water molecule in hemerythrin function

Cited by 8 publications

References 50 publications

Protonation of a Peroxodiiron(III) Complex and Conversion to a Diiron(III/IV) Intermediate: Implications for Proton-Assisted O–O Bond Cleavage in Nonheme Diiron Enzymes

Protonation of a Peroxodiiron(III) Complex and Conversion to a Diiron(III/IV) Intermediate: Implications for Proton-Assisted O–O Bond Cleavage in Nonheme Diiron Enzymes

Preparation of Au Electrodes Modified with Self-assembled Monolayers of Functional Metal Complexes

An Iron(II)[1,3‐bis(2′‐pyridylimino)isoindoline] Complex as a Catalyst for Substrate Oxidation with H₂O₂ – Evidence for a Transient Peroxidodiiron(III) Species

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Diiron(II) complexes showing a reversible oxygenation induced by a proton transfer mediated with a water molecule. Biological implication of a water molecule in hemerythrin function

Cited by 8 publications

References 50 publications

Protonation of a Peroxodiiron(III) Complex and Conversion to a Diiron(III/IV) Intermediate: Implications for Proton-Assisted O–O Bond Cleavage in Nonheme Diiron Enzymes

Protonation of a Peroxodiiron(III) Complex and Conversion to a Diiron(III/IV) Intermediate: Implications for Proton-Assisted O–O Bond Cleavage in Nonheme Diiron Enzymes

Preparation of Au Electrodes Modified with Self-assembled Monolayers of Functional Metal Complexes

An Iron(II)[1,3‐bis(2′‐pyridylimino)isoindoline] Complex as a Catalyst for Substrate Oxidation with H2O2 – Evidence for a Transient Peroxidodiiron(III) Species

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An Iron(II)[1,3‐bis(2′‐pyridylimino)isoindoline] Complex as a Catalyst for Substrate Oxidation with H₂O₂ – Evidence for a Transient Peroxidodiiron(III) Species