@article{oai:nagoya.repo.nii.ac.jp:00025140,
 author = {Onoda, Hiroki and Shoji, Osami and Suzuki, Kazuto and Sugimoto, Hiroshi and Shiro, Yoshitsugu and Watanabe, Yoshihito},
 journal = {Catalysis Science and Technology},
 month = {Jan},
 note = {Cytochrome P450 peroxygenases belonging to the CYP152 family catalyse the oxidation of fatty acids using H2O2. CYP152N1 isolated from Exiguobacterium sp. AT1b exclusively catalyses the α-selective hydroxylation of myristic acid at physiological H2O2 concentration. However, a series of shorter-alkyl-chain fatty acids such as tridecanoic acid were produced from myristic acid by increasing the concentration of H2O2 (1–10 mM). The yield of tridecanoic acid from myristic acid reached 17%. An 18O-labeled oxidant study suggested that CYP152N1 catalysed the overoxidation of α-hydroxymyristic acid to form α-ketomyristic acid, which in turn was spontaneously decomposed by H2O2 to yield tridecanoic acid. Crystal structure analysis of CYP152N1 revealed its high similarity to other CYP152 family enzymes, such as CYP152A1 and CYP152B1. MD simulations of α-hydroxymyristic acid accommodated in CYP152N1 proposed a possible pre-oxidation conformation of α-hydroxymyristic acid for the decarboxylation reaction.},
 pages = {434--442},
 title = {α-Oxidative decarboxylation of fatty acids catalysed by cytochrome P450 peroxygenases yielding shorter-alkyl-chain fatty acids},
 volume = {8},
 year = {2018}
}