Persulfidation
Modifying a protein amino acid by adding sulfur
From Wikipedia, the free encyclopedia
Persulfidation (also called sulfhydration) is a type of post-translational modification of proteins involving addition of a sulfur molecule onto a reactive thiol (-SH) group of a cysteine residue.[1] Persulfidation occurs in plants,[2] animals,[3] and throughout all kingdoms.[4] It is a redox mechanism that regulates diverse biological processes in hydrogen sulfide (H2S) signaling by regulating protein functions and/or subcellular localizations.[5][6]
The added sulfur atom (or atoms) are in a chain (R-S-SH, R-S-S-SH.[7] 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 (DTT) or TCEP, biological reducing agents such as glutathione, and proteins such as thioredoxin or glutaredoxin.[8][9]