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. 2019 Sep 2;10:3918. doi: 10.1038/s41467-019-11896-1

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 4 — Mutagenesis and comparison of oxygenase functions. a Site-directed mutagenesis of NorH. The active center of NorH/AurH model shows a hydrophobic pocket. Residues that may contribute to the different sizes of the cavity are presented in stick. The catalytic residue glutamine (orange) and the cofactor heme (yellow) are indicated. b The HPLC profile of authentic standard of aureothin (1), 7-OH-deoxyaureothin (3), deoxyaureothin (4), and NorH variants. UV detection is at 350 nm. c Schematic presentation of strategies to prepare hybrid NorH/AurH variants, and profiling of biotransformations. The hybrid NorH/AurH variants (left panel) correspond to HPLC profiles of extracts (right panel) of those variants. UV detection at 350 nm. d The HPLC profile of authentic standard of 2 and S. albus mutant strains. e AurH and NorH catalyze the biotransformation from 6 to 2