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From Alkanes to Carboxylic Acids: Terminal Oxygenation by a Fungal Peroxygenase
Author(s) -
Olmedo Andrés,
Aranda Carmen,
del Río José C.,
Kiebist Jan,
Scheibner Katrin,
Martínez Angel T.,
Gutiérrez Ana
Publication year - 2016
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201605430
Subject(s) - chemistry , hydroxylation , carboxylic acid , stereochemistry , cofactor , tetradecane , biocatalysis , organic chemistry , enzyme , reaction mechanism , catalysis
A new heme–thiolate peroxidase catalyzes the hydroxylation of n ‐alkanes at the terminal position—a challenging reaction in organic chemistry—with H 2 O 2 as the only cosubstrate. Besides the primary product, 1‐dodecanol, the conversion of dodecane yielded dodecanoic, 12‐hydroxydodecanoic, and 1,12‐dodecanedioic acids, as identified by GC–MS. Dodecanal could be detected only in trace amounts, and 1,12‐dodecanediol was not observed, thus suggesting that dodecanoic acid is the branch point between mono‐ and diterminal hydroxylation. Simultaneously, oxygenation was observed at other hydrocarbon chain positions (preferentially C2 and C11). Similar results were observed in reactions of tetradecane. The pattern of products formed, together with data on the incorporation of 18 O from the cosubstrate H 2 18 O 2 , demonstrate that the enzyme acts as a peroxygenase that is able to catalyze a cascade of mono‐ and diterminal oxidation reactions of long‐chain n ‐alkanes to give carboxylic acids.