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. 2016 Dec 1;22(2):185–207. doi: 10.1007/s00775-016-1414-3

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© The Author(s) 2016

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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.

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Fig. 8 — a Active site structure of a typical αKG dependent non-heme iron(II) dioxygenase, TauD, (PDB: 1OS7) and the mechanism of taurine hydroxylation catalyzed by TauD. b Active site structure of a representative non-heme diiron hydroxylase, soluble methane monooxygenase (sMMO) in reduced state (PDB: 1FYZ) and the typical mechanism of C–H hydroxylation catalyzed by non-heme diiron hydroxylase. Colors: iron (orange), oxygen (red), nitrogen (blue), sulfur (yellow)