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. 2019 Nov 14;9:16791. doi: 10.1038/s41598-019-53069-6

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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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Spectroscopic analysis of M. tuberculosis CysA2. (a) Circular dichroism spectra of CysA2 in absence and presence of co-substrates cyanide and thiosulfate. (b) Comparison of the secondary structure content of the recombinant CysA2 (CysA2r) with the structure deposited in PDB (CysA2 PDB 3HWI) and in presence of KCN (CysA2r + KCN). (c) Thermal unfolding of the protein monitored at 222 nm revealing a Tm of 58.3 °C. CysA2 is considered a stable protein. (d) Dynamic light scattering analysis of CysA2 in absence and presence of thiosulfate (Na₂S₂O₃), cyanide (KCN) and both. The results show that the substrates induced significant changes in the hydrodynamic radius, which is reduced just after addition of thiosulfate and cyanide (3.8 nm to 3.0), and it is reestablished after 10 minutes.