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Mimicking the Aromatic‐Ring‐Cleavage Activity of Gentisate‐1,2‐Dioxygenase by a Nonheme Iron Complex
Author(s) -
Rahaman Rubina,
Chakraborty Biswarup,
Paine Tapan Kanti
Publication year - 2016
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201607044
Subject(s) - dioxygenase , chemistry , gentisic acid , cleavage (geology) , stereochemistry , substrate (aquarium) , ring (chemistry) , bond cleavage , enzyme , catalysis , organic chemistry , biochemistry , fracture (geology) , oceanography , geotechnical engineering , engineering , salicylic acid , geology
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 O 2 , 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.