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. 2021 Oct 4;11:19004. doi: 10.1038/s41598-021-98433-7

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© The Author(s) 2022, corrected publication 2022

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Conformational examples of docking poses in which H6b [corresponding to trans-carveol (12), (A)], H3a [corresponding to cis-isopiperitenol (6), (B)], and H9b [the largest component of the byproduct docking pose group, (C)] of (S)-(−)-limonene contact the O atom bound to the Fe atom in heme. A view of the active site from the pocket entrance side. The heme and (S)-(−)-limonene are represented by orange and green sticks, respectively. The active site, heme oxygen is a red ball. The modification sites corresponding to H6b, H3a, and H9b are taken as magenta spheres. The orientation of the side chain ring of F87 (yellow stick) and the β-turn of T436-T438 (purple stick) changed depending on the modification sites on the substrate.