TY - GEN A1 - Olmedo, Andrés A1 - Aranda, Carmen A1 - Rio, José C. del A1 - Kiebist, Jan A1 - Scheibner, Katrin A1 - Martínez, Angel T. A1 - Gutiérrez, Ana T1 - From Alkanes to Carboxylic Acids: Terminal Oxygenation by a Fungal Peroxygenase T2 - Angewandte Chemie International Edition N2 - A new heme–thiolate peroxidase catalyzes the hydroxylation of n-alkanes at the terminal position—a challenging reaction in organic chemistry—with H2O2 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 18O from the cosubstrate H218O2, 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. KW - Peroxyenase Y1 - 2016 UR - http://onlinelibrary.wiley.com/doi/10.1002/anie.201605430/abstract U6 - https://doi.org/10.1002/anie.201605430 SN - 1521-3773 VL - 55 IS - 40 SP - 12248 EP - 12251 ER - TY - GEN A1 - Olmedo, Andrés A1 - Río, José C. del A1 - Kiebist, Jan A1 - Ullrich, René A1 - Hofrichter, Martin A1 - Scheibner, Katrin A1 - Martínez, Angel T. A1 - Gutiérrez, Ana T1 - Fatty Acid Chain Shortening by a Fungal Peroxygenase T2 - Chemistry A European Journal N2 - A recently discovered peroxygenase from the fungus Marasmius rotula (MroUPO) is able to catalyze the progressive one-carbon shortening of medium and longchain mono- and dicarboxylic acids by itself alone, in the presence of H₂O₂. The mechanism, analyzed using H₂O, starts with an a-oxidation catalyzed by MroUPO generat- ing an α-hydroxy acid, which is further oxidized by the enzyme to a reactive α-keto intermediate whose decarboxylation yields the one-carbon shorter fatty acid. Compared with the previously characterized peroxygenase of Agrocybe aegerita, a wider heme access channel, enabling fatty acid positioning with the carboxylic end near the heme cofactor (as seen in one of the crystal structures available) could be at the origin of the unique ability of MroUPO shortening carboxylic acid chains. KW - Peroxygenase Y1 - 2017 U6 - https://doi.org/10.1002/chem.201704773 SN - 1521-3765 SN - 0947-6539 VL - 23 SP - 16989 EP - 67 ER - TY - GEN A1 - Aranda, Carmen A1 - Olmedo, Andrés A1 - Kiebist, Jan A1 - Scheibner, Katrin A1 - Río, José C. del A1 - Martínez, Angel T. A1 - Gutiérrez, Ana T1 - Selective Epoxidation of Fatty Acids and Fatty Acid Methyl Esters by Fungal Peroxygenases T2 - CHEMCATCHEM N2 - Recently discovered fungal unspecific peroxygenases from Marasmius rotula and Chaetomium globosum catalyze the epoxidation of unsaturated fatty acids (FA) and FA methyl esters (FAME), unlike the well‐known peroxygenases from Agrocybe aegerita and Coprinopsis cinerea. Reactions of a series of unsaturated FA and FAME with cis‐configuration revealed high (up to 100 %) substrate conversion and selectivity towards epoxidation, although some significant differences were observed between enzymes and substrates with the best results being obtained with the C. globosum enzyme. This and the M. rotula peroxygenase appear as promising biocatalysts for the environmentally‐friendly production of reactive FA epoxides given their self‐sufficient monooxygenase activity and the high conversion rate and epoxidation selectivity. KW - Peroxygenase Y1 - 2018 U6 - https://doi.org/10.1002/cctc.201800849 SN - 1867-3899 VL - 10 IS - 18 SP - 3964 EP - 3968 ER -