Institute of Molecular Biotechnology, Graz University of Technology, NAWI Graz, 8010 Graz, Austria.
Institute of Chemistry, University of Graz, NAWI Graz, 8010 Graz, Austria.
Biomolecules. 2021 Nov 17;11(11):1708. doi: 10.3390/biom11111708.
Functionalisation of polycyclic aromatic hydrocarbons (PAHs) and their -heteroarene analogues (NPAHs) is a tedious synthetic endeavour that requires diverse bottom-up approaches. Cytochrome P450 enzymes of white-rot fungi were shown to participate in the fungal detoxification of xenobiotics and environmental hazards via hydroxylation of PAH compounds. In this paper, the recently discovered activity of the monooxygenase CYP5035S7 towards (N)PAHs was investigated in detail, and products formed from the substrates azulene, acenaphthene, fluorene, anthracene, and phenanthrene by whole-cell biocatalysis were isolated and characterised. The observed regioselectivity of CYP5035S7 could be explained by a combination of the substrate's electron density and steric factors influencing the substrate orientation giving insight into the active-site geometry of the enzyme.
多环芳烃（PAHs）及其杂芳烃类似物（NPAHs）的功能化是一项繁琐的合成工作，需要多种自下而上的方法。已经表明，白腐真菌中的细胞色素 P450 酶通过 PAH 化合物的羟化参与真菌对外源生物和环境危害的解毒。在本文中，详细研究了单加氧酶 CYP5035S7 对（N）PAHs 的最近发现的活性，并且通过全细胞生物催化从底物蓝烯、苊、芴、蒽和菲中分离和表征了形成的产物。CYP5035S7 观察到的区域选择性可以通过组合底物的电子密度和影响底物取向的空间因素来解释，这为酶的活性位点几何形状提供了深入了解。
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