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. 2019 Oct 28;10:4910. doi: 10.1038/s41467-019-12711-7

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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. 7 — The EGFD disulfide connectivity determines the degree of AspH-catalysed hydroxylation under non-redox conditions. End-point turnover reactions were performed as in the Methods Section. Light orange graphs represent controls in which AspH was replaced by buffer. a Schematic structure and calculated mass of the C_26mer peptide, bearing a canonical disulfide arrangement (Cys1–3, 2–4); disulfides are shown in green, the hydroxylation site (Asp103_hFX) is indicated in red. b No hydroxylation of the C_26mer peptide was observed under standard (non-redox) conditions; ~7% impurity (might correspond to an oxidized byproduct) was observed in this sample, including the control samples. c >95% Hydroxylation of the C_26mer peptide was observed under redox conditions. d Schematic structure and calculated mass of the NC_26mer peptide, bearing a non-canonical disulfide arrangement (Cys1–2, 3–4); disulfides are in green, the hydroxylation site (Asp103_hFX) is in red. e >95% Hydroxylation of the NC_26mer peptide was observed under standard (non-redox) conditions. f ~83% Hydroxylation of the NC_26mer peptide was observed under redox conditions