Oxidation of benzo(a)pyrene by extracellular ligninases of Phanerochaete chrysosporium. Veratryl alcohol and stability of ligninase.

Details

Serval ID
serval:BIB_A4535BF5A882
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Oxidation of benzo(a)pyrene by extracellular ligninases of Phanerochaete chrysosporium. Veratryl alcohol and stability of ligninase.
Journal
Journal of Biological Chemistry
Author(s)
Haemmerli S.D., Leisola M.S., Sanglard D., Fiechter A.
ISSN
0021-9258
Publication state
Published
Issued date
05/1986
Peer-reviewed
Oui
Volume
261
Number
15
Pages
6900-6903
Language
english
Abstract
Benzo(a)pyrene was oxidized with crude and purified extracellular ligninase preparations from Phanerochaete chrysosporium. Both the crude enzyme and the purified fractions oxidized the substrate to three organic soluble products, namely benzo(a)pyrene 1,6-, 3,6-, and 6,12-quinones. These findings support the recent proposition that lignin-degrading enzymes are peroxidases, mediating oxidation of aromatic compounds via aryl cation radicals. The ligninase which was unstable in the presence of hydrogen peroxide could be stabilized by addition of 3,4-dimethoxy benzyl alcohol to the reaction mixture. The oxidation of benzo(a)pyrene was enhanced in the presence of this alcohol.
Keywords
Basidiomycota/enzymology, Benzo(a)pyrene/metabolism, Benzyl Alcohols/pharmacology, Benzyl Compounds/pharmacology, Chromatography, High Pressure Liquid, Drug Stability, Kinetics, Oxidation-Reduction, Oxygenases/isolation & purification, Oxygenases/metabolism
Pubmed
Web of science
Create date
25/01/2008 15:40
Last modification date
20/08/2019 16:09
Usage data