Oxidation of cysteines Sample Clauses

Oxidation of cysteines. Reversible oxidation on reactive cysteines is the best characterized mechanism of redox- dependent signaling. Most cysteines have a pKa around 8 and are normally protonated under physiological pH, which renders them nonreactive. Cysteines with low pKa exist in thiolate anions state which is stabilized by nearby positively charged or aromatic side chains via charge-charge interactions. Thiolate anions are subject to various oxidative modification, including sulfenic acid (SOH), sulfinic acid (SO2H), sulfonic acid(SO3H), nitrylation (SNO), glutathionylation (SSG), and disulfide bond formation (S-S) (Figure I- 3) (37). Sulfenic acid is not stable and can readily form other species such as disulfide bond and sulfinic acid. Most modifications on cysteine (except for sulfonic acid) are reversible, by oxidoreductases, such as glutaredoxin or thioredoxin systems (37). These distinct reversible modifications may enable the processing of different redox signals and lead to unique protein functional changes and responses.
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