Million-fold activation of the [Fe2 (μ-O)2 ] diamond core for C-H bond cleavage

Genqiang Xue; Raymond De Hont; Eckard Münck; Lawrence Que

doi:10.1038/nchem.586

Million-fold activation of the [Fe₂ (μ-O)₂ ] diamond core for C-H bond cleavage

Genqiang Xue, Raymond De Hont, Eckard Münck, Lawrence Que

Chemistry (Twin Cities)

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

194 Scopus citations

Abstract

In biological systems, the cleavage of strong C-H bonds is often carried out by iron centres-such as that of methane monooxygenase in methane hydroxylation-through dioxygen activation mechanisms. High valent species with [Fe₂ (μ-O)₂ ] diamond cores are thought to act as the oxidizing moieties, but the synthesis of complexes that cleave strong C-H bonds efficiently has remained a challenge. We report here the conversion of a synthetic complex with a valence-delocalized [Fe^3.5 (μ-O) ₂ Fe^3.5]³⁺ diamond core (1) into a complex with a valence-localized [HO-Fe^III -O-Fe^IV =O]²⁺ open core (4), which cleaves C-H bonds over a million-fold faster. This activity enhancement results from three factors: the formation of a terminal oxoiron(iv) moiety, the conversion of the low-spin (S = 1) Fe^IV =O centre to a high-spin (S = 2) centre, and the concentration of the oxidizing capability to the active terminal oxoiron(iv) moiety. This suggests that similar isomerization strategies might be used by nonhaem diiron enzymes.

Original language	English (US)
Pages (from-to)	400-405
Number of pages	6
Journal	Nature Chemistry
Volume	2
Issue number	5
DOIs	https://doi.org/10.1038/nchem.586
State	Published - May 2010

Access

10.1038/nchem.586

OpenUrl availability

Full text

Cite this

@article{da154aaf7c754c86a7e473202c4cd213,

title = "Million-fold activation of the [Fe2 (μ-O)2 ] diamond core for C-H bond cleavage",

abstract = "In biological systems, the cleavage of strong C-H bonds is often carried out by iron centres-such as that of methane monooxygenase in methane hydroxylation-through dioxygen activation mechanisms. High valent species with [Fe2 (μ-O)2 ] diamond cores are thought to act as the oxidizing moieties, but the synthesis of complexes that cleave strong C-H bonds efficiently has remained a challenge. We report here the conversion of a synthetic complex with a valence-delocalized [Fe3.5 (μ-O) 2 Fe3.5]3+ diamond core (1) into a complex with a valence-localized [HO-FeIII -O-FeIV =O]2+ open core (4), which cleaves C-H bonds over a million-fold faster. This activity enhancement results from three factors: the formation of a terminal oxoiron(iv) moiety, the conversion of the low-spin (S = 1) FeIV =O centre to a high-spin (S = 2) centre, and the concentration of the oxidizing capability to the active terminal oxoiron(iv) moiety. This suggests that similar isomerization strategies might be used by nonhaem diiron enzymes.",

author = "Genqiang Xue and {De Hont}, Raymond and Eckard M{\"u}nck and Lawrence Que",

year = "2010",

month = may,

doi = "10.1038/nchem.586",

language = "English (US)",

volume = "2",

pages = "400--405",

journal = "Nature Chemistry",

issn = "1755-4330",

publisher = "Nature Publishing Group",

number = "5",

}

TY - JOUR

T1 - Million-fold activation of the [Fe2 (μ-O)2 ] diamond core for C-H bond cleavage

AU - Xue, Genqiang

AU - De Hont, Raymond

AU - Münck, Eckard

AU - Que, Lawrence

PY - 2010/5

Y1 - 2010/5

N2 - In biological systems, the cleavage of strong C-H bonds is often carried out by iron centres-such as that of methane monooxygenase in methane hydroxylation-through dioxygen activation mechanisms. High valent species with [Fe2 (μ-O)2 ] diamond cores are thought to act as the oxidizing moieties, but the synthesis of complexes that cleave strong C-H bonds efficiently has remained a challenge. We report here the conversion of a synthetic complex with a valence-delocalized [Fe3.5 (μ-O) 2 Fe3.5]3+ diamond core (1) into a complex with a valence-localized [HO-FeIII -O-FeIV =O]2+ open core (4), which cleaves C-H bonds over a million-fold faster. This activity enhancement results from three factors: the formation of a terminal oxoiron(iv) moiety, the conversion of the low-spin (S = 1) FeIV =O centre to a high-spin (S = 2) centre, and the concentration of the oxidizing capability to the active terminal oxoiron(iv) moiety. This suggests that similar isomerization strategies might be used by nonhaem diiron enzymes.

AB - In biological systems, the cleavage of strong C-H bonds is often carried out by iron centres-such as that of methane monooxygenase in methane hydroxylation-through dioxygen activation mechanisms. High valent species with [Fe2 (μ-O)2 ] diamond cores are thought to act as the oxidizing moieties, but the synthesis of complexes that cleave strong C-H bonds efficiently has remained a challenge. We report here the conversion of a synthetic complex with a valence-delocalized [Fe3.5 (μ-O) 2 Fe3.5]3+ diamond core (1) into a complex with a valence-localized [HO-FeIII -O-FeIV =O]2+ open core (4), which cleaves C-H bonds over a million-fold faster. This activity enhancement results from three factors: the formation of a terminal oxoiron(iv) moiety, the conversion of the low-spin (S = 1) FeIV =O centre to a high-spin (S = 2) centre, and the concentration of the oxidizing capability to the active terminal oxoiron(iv) moiety. This suggests that similar isomerization strategies might be used by nonhaem diiron enzymes.

UR - http://www.scopus.com/inward/record.url?scp=77951693360&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77951693360&partnerID=8YFLogxK

U2 - 10.1038/nchem.586

DO - 10.1038/nchem.586

M3 - Article

C2 - 20414242

AN - SCOPUS:77951693360

SN - 1755-4330

VL - 2

SP - 400

EP - 405

JO - Nature Chemistry

JF - Nature Chemistry

IS - 5

ER -

Million-fold activation of the [Fe₂ (μ-O)₂ ] diamond core for C-H bond cleavage

Abstract

Access

OpenUrl availability

Other files and links

Fingerprint

Cite this