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. 2017 Aug 30;7:9938. doi: 10.1038/s41598-017-09275-1

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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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Identification of HNO-modified cysteines in PKGIα by NOxICAT. (A) Exposure of recombinant human PKGIα to HNO donors induced oxidation of Cys42, Cys117 and Cys195 in PKGIα. The table summarises the mass charge (m/z) in molecular ions (mi) of the detected peptides containing the cysteines in the reduced (blue) and oxidised (pink) state. (B) Fourier Transform Mass Spectrometry spectra are expressed as the relative abundance of the detected peptides in m/z containing Cys42 (left), Cys117 (middle) and Cys195 (right), vehicle-treated (top), after exposure to 1-nitrosocyclohexyl acetate (NCA; 25 mmol/L, 15 min) (middle) or Angeli’s salt (AS; 25 µmol/L, 15 min) (bottom). (C) Quantification of the detected oxidised (pink) versus reduced (blue) peptide fraction is shown as percent of the total detected peptides.