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. 2018 Sep 11;8:13576. doi: 10.1038/s41598-018-31851-2

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© The Author(s) 2018

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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Solubilization of the TorC cytochrome under mild conditions. Peroxidase activity of c type hemes of cytochromes from membranous and membrane extracted proteins of S. oneidensis wild type cells (WT) or ΔtorE deletion mutant (ΔE) either after 2% DDM solubilization or 1.5 M NaBr. Ten microgram proteins were loaded in each lane of the 3–14% SDS gel. After electrophoresis, c-type cytochromes were revealed by their peroxidase activity. TorC is indicated by an arrow. **T test analysis performed by GraphPad Prism Software shows that data from three replicates are significantly different (p = 0.0058). No band can be detected in the WT lanes for three replicated experiments, preventing statistical analyses Separated portions of the same blots are represented with their respective molecular weight markers (see Figure S2).