Chlorination and cleavage of lignin structures by funal chloroperoxidases

Two fungal chloroperoxidases (CPOs), the heme enzyme from Caldariomyces fumago and the vanadium enzyme from Curvularia inaequalis, chlorinated 1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane, a dimeric model compound that represents the major nonphenolic structure in lignin. B...

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Bibliographic Details
Published in:Applied and environmental microbiology 2003-08, Vol.69 (8), p.5015
Main Authors: Ortiz-Bermudez, Patricia, Srebotnik, Ewald, Hammel, Kenneth E
Format: Article
Language:English
Subjects:
Fungi
Microbiology
Pathogens
Soils
Online Access:Get full text
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Summary:Two fungal chloroperoxidases (CPOs), the heme enzyme from Caldariomyces fumago and the vanadium enzyme from Curvularia inaequalis, chlorinated 1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane, a dimeric model compound that represents the major nonphenolic structure in lignin. Both enzymes also cleaved this dimer to give 1-chloro-4-ethoxy-3-methoxybenzene and 1,2-dichloro-4-ethoxy-5-methoxybenzene, and they depolymerized a synthetic guaiacyl lignin. Since fungal CPOs occur in soils and the fungi that produce them are common inhabitants of plant debris, CPOs may have roles in the natural production of high-molecular-weight chloroaromatics and in lignin breakdown. [PERIODICAL ABSTRACT]
ISSN:0099-2240
1098-5336