# Persulfidation

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{{Short description|Modifying a protein amino acid by adding sulfur}}

'''Persulfidation''' (also called '''sulfhydration''') is a type of [post-translational modification](/source/post-translational_modification) of proteins involving addition of a sulfur molecule onto a reactive [thiol](/source/thiol) (-SH) group of a [cysteine](/source/cysteine) residue.<ref>M.R. Filipovic, Persulfidation (S-sulfhydration) and H2S. Handbook of experimental pharmacology 230 (2015) 29-59</ref> Persulfidation occurs in plants,<ref>A. Aroca, A. Serna, C. Gotor, and L. Romero, C., S-sulfhydration: a cysteine posttranslational modification in plant systems. Plant Physiology 168 (2015) 334-342</ref> animals,<ref>.K. Mustafa, M.M. Gadalla, N. Sen, S. Kim, W. Mu, S.K. Gazi, R.K. Barrow, G. Yang, R. Wang, and S.H. Snyder, H<sub>2</sub>S Signals Through Protein S-Sulfhydration. Sci. Signal. 2 (2009) ra72</ref> and throughout all [kingdoms](/source/Kingdom_(biology)).<ref>Zivanovic J, Kouroussis E, Kohl JB, Adhikari B, Bursac B, Schott-Roux S, Petrovic D, Miljkovic JL, Thomas-Lopez D, Jung Y, Miler M, Mitchell S, Milosevic V, Gomes JE, Benhar M, Gonzalez-Zorn B, Ivanovic-Burmazovic I, Torregrossa R, Mitchell JR, Whiteman M, Schwarz G, Snyder SH, Paul BD, Carroll KS, Filipovic MR. Selective Persulfide Detection Reveals Evolutionarily Conserved Antiaging Effects of S-Sulfhydration. Cell Metab. 30(6), 1152-1170 (2019)</ref> It is a [redox](/source/redox) mechanism that regulates diverse biological processes in [hydrogen sulfide](/source/hydrogen_sulfide) (H<sub>2</sub>S) signaling by regulating protein functions and/or subcellular localizations.<ref>A. Aroca, C. Gotor, and L.C. Romero, Hydrogen Sulfide Signaling in Plants: Emerging Roles of Protein Persulfidation. Frontiers in plant science 9 (2018)</ref><ref>Filipovic MR, Zivanovic J, Alvarez B, Banerjee R. Chemical Biology of H(2)S Signaling through Persulfidation. Chem Rev. 118(3), 1253-1337 (2018)</ref>

The added sulfur atom (or atoms) are in a chain (R-S-SH, R-S-S-SH.<ref>{{cite journal | url=https://doi.org/10.1089/ars.2019.7889 | doi=10.1089/ars.2019.7889 | title=S-Persulfidation: Chemistry, Chemical Biology, and Significance in Health and Disease | date=2020 | last1=Yang | first1=Chun-tao | last2=Devarie-Baez | first2=Nelmi O. | last3=Hamsath | first3=Akil | last4=Fu | first4=Xiao-Dong | last5=Xian | first5=Ming | journal=Antioxidants & Redox Signaling | volume=33 | issue=15 | pages=1092–1114 | pmid=31547682 | pmc=7583347 }}</ref> These sulfur chains are unstable and react readily, making identification and quantification difficult.

This modification can be reversed back into a thiol by exogenous chemical reducing agents such as [dithiothreitol](/source/dithiothreitol) (DTT) or [TCEP](/source/TCEP), biological reducing agents such as [glutathione](/source/glutathione), and proteins such as [thioredoxin](/source/thioredoxin) or [glutaredoxin](/source/glutaredoxin).<ref>Wedmann R, Onderka C, Wei S, Szijártó IA, Miljkovic JL, Mitrovic A, Lange M, Savitsky S, Yadav PK, Torregrossa R, Harrer EG, Harrer T, Ishii I, Gollasch M, Wood ME, Galardon E, Xian M, Whiteman M, Banerjee R, Filipovic MR. Improved tag-switch method reveals that thioredoxin acts as depersulfidase and controls the intracellular levels of protein persulfidation. Chem Sci. 7(5), 3414-3426 (2016)</ref><ref>É. Dóka, I. Pader, A. Bíró, K. Johansson, Q. Cheng, K. Ballagó, J.R. Prigge, D. Pastor-Flores, T.P. Dick, E.E. Schmidt, E.S.J. Arnér, and P. Nagy, A novel persulfide detection method reveals protein persulfide- and polysulfide-reducing functions of thioredoxin and glutathione systems. Science Advances 2 (2016)</ref>

== References ==
{{reflist}}

Category:Sulfur
Category:Post-translational modification

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Adapted from the Wikipedia article [Persulfidation](https://en.wikipedia.org/wiki/Persulfidation) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/Persulfidation?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.