Sulfhydryl groups on protein Cys residues undergo an array of oxidative reactions and modifications, giving rise to a virtual redox zip code with physiological and pathophysiological relevance for modulation of protein structure and functions. While over two decades of studies have established NO-dependent S-nitrosylation as ubiquitous and fundamental for the regulation of diverse protein activities, proteomic methods for studying H2S-dependent S-sulfhydration have only recently been described and now suggest that this is also an abundant modification with potential for global physiological importance. Notably, protein S-sulfhydration and S-nitrosylation bear striking similarities in terms of their chemical and biological determinants, as well as reversal of these modifications via group-transfer to glutathione, followed by the removal from glutathione by enzymes that have apparently evolved to selectively catalyze denitrosylation and desulfhydration. Here we review determinants of protein and low-molecular-weight thiol S-sulfhydration/desulfhydration, similarities with S-nitrosylation/denitrosylation, and methods that are being employed to investigate and quantify these gasotransmitter-mediated cell signaling systems.
Keywords: (N-[(6-biotinamido) hexyl]-3′-(2′-pyridyldithio) propionamide); 2-(4-carboxyphenyl)-4,5-dihydro-4,4,5,5-tetramethyl-1H-imidazolyl-1-oxy-3-oxide; Biotin Switch; Biotin-HPDP; CBS; CSE; Cysteine; ETHE1; GSNO; GSSH; Glutathione; Hydrogen sulfide; MMTS; MS/MS; MST; Nitric oxide; Persulfide; S-nitrosoglutathione; SH; SNOSID; SQR; SRB; Sulfhydration; Sulfhydryl; TST; carboxy-PTIO; cystathionine β-synthase; cystathionine γ-lyase; glutathione persulfide; mercaptopyruvate sulfurtransferase; methyl methane thiosulfonate; persulfide dioxygenase; sulfate reducing bacteria; sulfide quinone reductase; tandem mass spectrometry; thiol; thiosulfate sulfur transferase (a.k.a. rhodanese).
Copyright © 2013 The Authors. Published by Elsevier Inc. All rights reserved.