Dioxygen binding to complexes with FeII2(μOH) 2 cores: Steric control of activation barriers and O 2-adduct formation

Sergey V. Kryatov; Sonia Taktak; Ivan V. Korendovych; Elena V. Rybak-Akimova; József Kaizer; Stéphane Torelli; Xiaopeng Shan; Sanjay Mandal; Vicki L. MacMurdo; Antoni Mairata I Payeras; Lawrence Que

doi:10.1021/ic0485312

Dioxygen binding to complexes with Fe^II₂(μOH) ₂ cores: Steric control of activation barriers and O ₂-adduct formation

Sergey V. Kryatov, Sonia Taktak, Ivan V. Korendovych, Elena V. Rybak-Akimova, József Kaizer, Stéphane Torelli, Xiaopeng Shan, Sanjay Mandal, Vicki L. MacMurdo, Antoni Mairata I Payeras, Lawrence Que

Research output: Contribution to journal › Article › peer-review

82 Scopus citations

Abstract

A series of complexes with [Fe^II₂(μ-OH) ₂] cores has been synthesized with N3 and N4 ligands and structurally characterized to serve as models for nonheme diiron(II) sites in enzymes that bind and activate O₂. These complexes react with O₂ in solution via bimolecular rate-limiting steps that differ in rate by 10 ³-fold, depending on ligand denticity and steric hindrance near the diiron center. Low-temperature trapping of a (μ-oxo)(μ-1,2-peroxo) diiron(III) intermediate after O₂ binding requires sufficient steric hindrance around the diiron center and the loss of a proton (presumably that of a hydroxo bridge or a yet unobserved hydroperoxo intermediate). The relative stability of these and other (μ-1,2-peroxo)diiron(III) intermediates suggests that these species may not be on the direct pathway for dioxygen activation.

Original language	English (US)
Pages (from-to)	85-99
Number of pages	15
Journal	Inorganic Chemistry
Volume	44
Issue number	1
DOIs	https://doi.org/10.1021/ic0485312
State	Published - Jan 10 2005
Externally published	Yes

ASJC Scopus subject areas

Physical and Theoretical Chemistry
Inorganic Chemistry

Access to Document

10.1021/ic0485312

Cite this

@article{12c4cf06b67b43a28992836687832b74,

title = "Dioxygen binding to complexes with FeII2(μOH) 2 cores: Steric control of activation barriers and O 2-adduct formation",

abstract = "A series of complexes with [FeII2(μ-OH) 2] cores has been synthesized with N3 and N4 ligands and structurally characterized to serve as models for nonheme diiron(II) sites in enzymes that bind and activate O2. These complexes react with O2 in solution via bimolecular rate-limiting steps that differ in rate by 10 3-fold, depending on ligand denticity and steric hindrance near the diiron center. Low-temperature trapping of a (μ-oxo)(μ-1,2-peroxo) diiron(III) intermediate after O2 binding requires sufficient steric hindrance around the diiron center and the loss of a proton (presumably that of a hydroxo bridge or a yet unobserved hydroperoxo intermediate). The relative stability of these and other (μ-1,2-peroxo)diiron(III) intermediates suggests that these species may not be on the direct pathway for dioxygen activation.",

author = "Kryatov, {Sergey V.} and Sonia Taktak and Korendovych, {Ivan V.} and Rybak-Akimova, {Elena V.} and J{\'o}zsef Kaizer and St{\'e}phane Torelli and Xiaopeng Shan and Sanjay Mandal and MacMurdo, {Vicki L.} and {Mairata I Payeras}, Antoni and Lawrence Que",

year = "2005",

month = jan,

day = "10",

doi = "10.1021/ic0485312",

language = "English (US)",

volume = "44",

pages = "85--99",

journal = "Inorganic Chemistry",

issn = "0020-1669",

publisher = "American Chemical Society",

number = "1",

}

TY - JOUR

T1 - Dioxygen binding to complexes with FeII2(μOH) 2 cores

T2 - Steric control of activation barriers and O 2-adduct formation

AU - Kryatov, Sergey V.

AU - Taktak, Sonia

AU - Korendovych, Ivan V.

AU - Rybak-Akimova, Elena V.

AU - Kaizer, József

AU - Torelli, Stéphane

AU - Shan, Xiaopeng

AU - Mandal, Sanjay

AU - MacMurdo, Vicki L.

AU - Mairata I Payeras, Antoni

AU - Que, Lawrence

PY - 2005/1/10

Y1 - 2005/1/10

N2 - A series of complexes with [FeII2(μ-OH) 2] cores has been synthesized with N3 and N4 ligands and structurally characterized to serve as models for nonheme diiron(II) sites in enzymes that bind and activate O2. These complexes react with O2 in solution via bimolecular rate-limiting steps that differ in rate by 10 3-fold, depending on ligand denticity and steric hindrance near the diiron center. Low-temperature trapping of a (μ-oxo)(μ-1,2-peroxo) diiron(III) intermediate after O2 binding requires sufficient steric hindrance around the diiron center and the loss of a proton (presumably that of a hydroxo bridge or a yet unobserved hydroperoxo intermediate). The relative stability of these and other (μ-1,2-peroxo)diiron(III) intermediates suggests that these species may not be on the direct pathway for dioxygen activation.

AB - A series of complexes with [FeII2(μ-OH) 2] cores has been synthesized with N3 and N4 ligands and structurally characterized to serve as models for nonheme diiron(II) sites in enzymes that bind and activate O2. These complexes react with O2 in solution via bimolecular rate-limiting steps that differ in rate by 10 3-fold, depending on ligand denticity and steric hindrance near the diiron center. Low-temperature trapping of a (μ-oxo)(μ-1,2-peroxo) diiron(III) intermediate after O2 binding requires sufficient steric hindrance around the diiron center and the loss of a proton (presumably that of a hydroxo bridge or a yet unobserved hydroperoxo intermediate). The relative stability of these and other (μ-1,2-peroxo)diiron(III) intermediates suggests that these species may not be on the direct pathway for dioxygen activation.

UR - http://www.scopus.com/inward/record.url?scp=19944429115&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=19944429115&partnerID=8YFLogxK

U2 - 10.1021/ic0485312

DO - 10.1021/ic0485312

M3 - Article

C2 - 15627364

AN - SCOPUS:19944429115

SN - 0020-1669

VL - 44

SP - 85

EP - 99

JO - Inorganic Chemistry

JF - Inorganic Chemistry

IS - 1

ER -

Dioxygen binding to complexes with Fe^II₂(μOH) ₂ cores: Steric control of activation barriers and O ₂-adduct formation

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this