Mimicking the Aromatic-Ring-Cleavage Activity of Gentisate-1,2-Dioxygenase by a Nonheme Iron Complex

Rubina Rahaman; Biswarup Chakraborty; Tapan Kanti Paine

doi:10.1002/anie.201607044

Mimicking the Aromatic-Ring-Cleavage Activity of Gentisate-1,2-Dioxygenase by a Nonheme Iron Complex

Rubina Rahaman, Biswarup Chakraborty, Tapan Kanti Paine

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

18 Scopus citations

Abstract

Gentisate-1,2-dioxygenase (GDO), a nonheme iron enzyme in the cupin superfamily, catalyzes the cleavage of the aromatic-ring of 2,5-dihydroxybenzoic acid (gentisic acid) to form maleylpyruvic acid in the microbial aerobic degradation of aromatic compounds. To develop a functional model of GDO, we have isolated a nonheme iron(II) complex, [(Tp^Ph2)Fe^II(DHN-H)] (Tp^Ph2=hydrotris(3,5-diphenylpyrazole-1-yl)borate, DHN-H=1,4-dihydroxy-2-naphthoate). In the reaction with O₂, the biomimetic complex oxidatively cleaves the aromatic ring of the coordinated substrate with the incorporation of both the oxygen atoms from molecular oxygen into the cleavage product. The presence of para-hydroxy group on the substrate plays a crucial role in directing the aromatic-ring cleaving reaction.

Original language	English
Pages (from-to)	13838-13842
Number of pages	5
Journal	Angewandte Chemie - International Edition
Volume	55
Issue number	44
DOIs	https://doi.org/10.1002/anie.201607044
State	Published - 24 Oct 2016
Externally published	Yes

Keywords

C−C bond cleavage
biomimetic models
dioxygen
gentisate
iron complexes

ASJC Scopus subject areas

Catalysis
General Chemistry

Access to Document

10.1002/anie.201607044

Cite this

@article{6514c3c1c0474d9d9a3d44ee49845131,

title = "Mimicking the Aromatic-Ring-Cleavage Activity of Gentisate-1,2-Dioxygenase by a Nonheme Iron Complex",

abstract = "Gentisate-1,2-dioxygenase (GDO), a nonheme iron enzyme in the cupin superfamily, catalyzes the cleavage of the aromatic-ring of 2,5-dihydroxybenzoic acid (gentisic acid) to form maleylpyruvic acid in the microbial aerobic degradation of aromatic compounds. To develop a functional model of GDO, we have isolated a nonheme iron(II) complex, [(TpPh2)FeII(DHN-H)] (TpPh2=hydrotris(3,5-diphenylpyrazole-1-yl)borate, DHN-H=1,4-dihydroxy-2-naphthoate). In the reaction with O2, the biomimetic complex oxidatively cleaves the aromatic ring of the coordinated substrate with the incorporation of both the oxygen atoms from molecular oxygen into the cleavage product. The presence of para-hydroxy group on the substrate plays a crucial role in directing the aromatic-ring cleaving reaction.",

keywords = "C−C bond cleavage, biomimetic models, dioxygen, gentisate, iron complexes",

author = "Rubina Rahaman and Biswarup Chakraborty and Paine, {Tapan Kanti}",

note = "Publisher Copyright: {\textcopyright} 2016 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim",

year = "2016",

month = oct,

day = "24",

doi = "10.1002/anie.201607044",

language = "English",

volume = "55",

pages = "13838--13842",

journal = "Angewandte Chemie - International Edition",

issn = "1433-7851",

publisher = "John Wiley and Sons Ltd",

number = "44",

}

TY - JOUR

T1 - Mimicking the Aromatic-Ring-Cleavage Activity of Gentisate-1,2-Dioxygenase by a Nonheme Iron Complex

AU - Rahaman, Rubina

AU - Chakraborty, Biswarup

AU - Paine, Tapan Kanti

PY - 2016/10/24

Y1 - 2016/10/24

N2 - Gentisate-1,2-dioxygenase (GDO), a nonheme iron enzyme in the cupin superfamily, catalyzes the cleavage of the aromatic-ring of 2,5-dihydroxybenzoic acid (gentisic acid) to form maleylpyruvic acid in the microbial aerobic degradation of aromatic compounds. To develop a functional model of GDO, we have isolated a nonheme iron(II) complex, [(TpPh2)FeII(DHN-H)] (TpPh2=hydrotris(3,5-diphenylpyrazole-1-yl)borate, DHN-H=1,4-dihydroxy-2-naphthoate). In the reaction with O2, the biomimetic complex oxidatively cleaves the aromatic ring of the coordinated substrate with the incorporation of both the oxygen atoms from molecular oxygen into the cleavage product. The presence of para-hydroxy group on the substrate plays a crucial role in directing the aromatic-ring cleaving reaction.

AB - Gentisate-1,2-dioxygenase (GDO), a nonheme iron enzyme in the cupin superfamily, catalyzes the cleavage of the aromatic-ring of 2,5-dihydroxybenzoic acid (gentisic acid) to form maleylpyruvic acid in the microbial aerobic degradation of aromatic compounds. To develop a functional model of GDO, we have isolated a nonheme iron(II) complex, [(TpPh2)FeII(DHN-H)] (TpPh2=hydrotris(3,5-diphenylpyrazole-1-yl)borate, DHN-H=1,4-dihydroxy-2-naphthoate). In the reaction with O2, the biomimetic complex oxidatively cleaves the aromatic ring of the coordinated substrate with the incorporation of both the oxygen atoms from molecular oxygen into the cleavage product. The presence of para-hydroxy group on the substrate plays a crucial role in directing the aromatic-ring cleaving reaction.

KW - C−C bond cleavage

KW - biomimetic models

KW - dioxygen

KW - gentisate

KW - iron complexes

UR - http://www.scopus.com/inward/record.url?scp=84992111852&partnerID=8YFLogxK

U2 - 10.1002/anie.201607044

DO - 10.1002/anie.201607044

M3 - Article

AN - SCOPUS:84992111852

SN - 1433-7851

VL - 55

SP - 13838

EP - 13842

JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 44

ER -

Mimicking the Aromatic-Ring-Cleavage Activity of Gentisate-1,2-Dioxygenase by a Nonheme Iron Complex

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this