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General Health & Fitness
Nutrition and Supplements
The mechanism of action of N-acetylcysteine (NAC)
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<blockquote data-quote="madman" data-source="post: 208896" data-attributes="member: 13851"><p><strong>Fig. 7. <u>Three hypotheses potentially explaining persulfide-mediated cytoprotection</u>. (A) The first hypothesis argues that persulfidation of Cys residues on proteins changes their activity and/or signaling properties in an adaptive manner, e.g. to alter metabolism or gene expression. (B) The second hypothesis argues that protein persulfidation protects thiol groups against irreversible oxidative damage. While sulfinic (SO2H) and sulfonic (SO3H) acid residues cannot be repaired, perthiosulfinic (SSO2H) and perthiosulfonic (SSO3H) acid residues are easily repaired by a disulfide reductase, such as thioredoxin (TRX). Reduction regenerates the original thiol and presumably releases the outer sulfur as sulfur dioxide (SO2) or sulfite (SO3 2-). (C) The third hypothesis argues for a scavenging role of (low-molecular-weight) persulfides, as they are more reactive towards one- and two-electron oxidants than thiols. This is explained by (i) the α-effect, which increases the nucleophilicity of the persulfide’s outer sulfur atom, and (ii) for two-electron oxidants, the higher availability of the reactive thiolate (i.e., lower pKa). In addition, persulfides are proposed to act as highly efficient radical scavengers. They form stable perthiyl radicals, unable to propagate radical chain reactions, and capable of recombining into tetrasulfides, thereby eliminating radicals from the system.</strong></p><p><strong>[ATTACH=full]16736[/ATTACH]</strong></p></blockquote><p></p>
[QUOTE="madman, post: 208896, member: 13851"] [B]Fig. 7. [U]Three hypotheses potentially explaining persulfide-mediated cytoprotection[/U]. (A) The first hypothesis argues that persulfidation of Cys residues on proteins changes their activity and/or signaling properties in an adaptive manner, e.g. to alter metabolism or gene expression. (B) The second hypothesis argues that protein persulfidation protects thiol groups against irreversible oxidative damage. While sulfinic (SO2H) and sulfonic (SO3H) acid residues cannot be repaired, perthiosulfinic (SSO2H) and perthiosulfonic (SSO3H) acid residues are easily repaired by a disulfide reductase, such as thioredoxin (TRX). Reduction regenerates the original thiol and presumably releases the outer sulfur as sulfur dioxide (SO2) or sulfite (SO3 2-). (C) The third hypothesis argues for a scavenging role of (low-molecular-weight) persulfides, as they are more reactive towards one- and two-electron oxidants than thiols. This is explained by (i) the α-effect, which increases the nucleophilicity of the persulfide’s outer sulfur atom, and (ii) for two-electron oxidants, the higher availability of the reactive thiolate (i.e., lower pKa). In addition, persulfides are proposed to act as highly efficient radical scavengers. They form stable perthiyl radicals, unable to propagate radical chain reactions, and capable of recombining into tetrasulfides, thereby eliminating radicals from the system. [ATTACH type="full" alt="Screenshot (7629).png"]16736[/ATTACH][/B] [/QUOTE]
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General Health & Fitness
Nutrition and Supplements
The mechanism of action of N-acetylcysteine (NAC)
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