Pyridine as novel substrate for regioselective oxygenation with aromatic peroxygenase from Agrocybe aegerita
Pyridine as novel substrate for regioselective oxygenation with aromatic peroxygenase from Agrocybe aegerita
复制标题
DOI：
10.1016/j.febslet.2008.11.006
复制
发表时间：
2008-12-10
期刊：
影响因子：
3.5
通讯作者：
Hofrichter, Martin
中科院分区：
文献类型：
--
作者：
Ullrich, Rene;Dolge, Christoph;Hofrichter, Martin
杨树菇过氧化物酶（AaP）是一种多功能的胞外生物催化剂，能够氧化芳香族化合物。在此，我们报道了吡啶（PY）的选择性氧化，其唯一产物为吡啶N - 氧化物。以¹⁸O₂H₂作为共底物，证实氧的来源是过氧化物。因此，AaP可被视为一种真正的过氧合酶，它将一个氧原子从过氧化物转移到底物上。据我们所知，只有两种类型的酶能在氮原子处氧化吡啶：细菌甲烷单加氧酶和少数细胞色素P450单加氧酶。AaP是第一种催化此反应的胞外酶和过氧化物酶，并且它还能将取代吡啶转化为相应的N - 氧化物。（C）2008欧洲生物化学学会联合会。由爱思唯尔出版集团出版。保留所有权利。
Agrocybe aegerita peroxidase (AaP) is a versatile extracellular biocatalyst that can oxygenate aromatic compounds. Here, we report on the selective oxidation of pyridine (PY) yielding pyridine N-oxide as sole product. Using (H2O2)-O-18 as co-substrate, the origin of oxygen was confirmed to be the peroxide. Therefore, AaP can be regarded as a true peroxygenase transferring one oxygen atom from peroxide to the substrate. To our best knowledge, there are only two types of enzymes oxidizing PY at the nitrogen: bacterial methane monooxygenase and a few P450 monooxygenases. AaP is the first extracellular enzyme and the first peroxidase that catalyzes this reaction, and it converted also substituted PYs into the corresponding N-oxides. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.