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. 2023 Feb 9;12(2):423. doi: 10.3390/antiox12020423

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© 2023 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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H₂S_n acted on the cysteines of PerR. (A) The Cys¹⁹–SSH group was blocked by IAM in the peptide 1 from H₂S_n–treated PerR. (B) The Cys¹⁹–SH group was blocked by IAM in the peptide 2 from DTT-treated PerR. (C) The Cys¹²¹–SSH group was blocked by IAM in the peptide 3 from H₂S_n-treated PerR. (D) The Cys¹²¹–SH group was blocked by IAM in the peptide 4 from DTT–treated PerR. The purified PerR (5 mg/mL) was treated with 1 mM H₂S_n and 1 mM DTT for 30 min, at 25 °C. After denaturing and incubating with IAM, the reacted protein was digested by trypsin. The generated peptides were detected by LTQ-Orbitrap tandem mass spectrometry.