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. 2017 Apr 26;7:1195. doi: 10.1038/s41598-017-01179-4

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© The Author(s) 2017

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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Overview of the percentages of thiol-oxidation levels of all Cys peptides identified in the redox proteome of the M. smegmatis wild type and the mshC mutant under control and NaOCl stress as revealed by OxICAT. Reduced Cys peptides with a <25% oxidation are shown in green including those <10% oxidized (blue) and 10–25% oxidized (magenta). Cys peptides with an oxidation degree of >25% and >75% are shown in yellow and red, respectively. The percentage of thiol-oxidation increase is shown with an orange-brown color gradient including Cys peptides with 10–20% and >20% increased oxidation by NaOCl stress. The mshC mutant shows a higher basal level oxidation in the control that resembles that of the wild type after NaOCl stress.