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 journalArticlepeer-review

16 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, [(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.

Original languageEnglish
Pages (from-to)13838-13842
Number of pages5
JournalAngewandte Chemie - International Edition
Volume55
Issue number44
DOIs
StatePublished - 24 Oct 2016
Externally publishedYes

Keywords

  • C−C bond cleavage
  • biomimetic models
  • dioxygen
  • gentisate
  • iron complexes

ASJC Scopus subject areas

  • Catalysis
  • Chemistry (all)

Fingerprint

Dive into the research topics of 'Mimicking the Aromatic-Ring-Cleavage Activity of Gentisate-1,2-Dioxygenase by a Nonheme Iron Complex'. Together they form a unique fingerprint.

Cite this