[Show abstract][Hide abstract] ABSTRACT: Thiol redox chemical reactions play a key role in a variety of physiological processes, mainly due to the presence of low-molecular-weight thiols and cysteine residues in pro-teins involved in catalysis and regulation. Specifically, the subtle sensitivity of thiol reactivity to the environment makes the use of simulation techniques extremely valuable for obtaining microscopic insights. In this work we review the application of classical and quantum–mechanical atomistic simulation tools to the investigation of selected relevant issues in thiol redox biochemistry, such as investigations on (1) the protonation state of cysteine in protein, (2) two-electron oxi-dation of thiols by hydroperoxides, chloramines, and hypochlorous acid, (3) mechanistic and kinetics aspects of the de novo formation of disulfide bonds and thiol−disulfide exchange, (4) formation of sulfenamides, (5) formation of nitrosothiols and transnitrosation reactions, and (6) one-electron oxidation pathways. CysS -Cysteinate CysSOH Cysteine sulfenic acid DFT Density functional theory GPx Glutathione peroxidase GSH Glutathione MD Molecular dynamics MM Molecular mechanics Prx Peroxiredoxin QM Quantum mechanics ROS Reactive oxygen species Introduction
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Keehyoung Joo, InSuk Joung, Jinhyuk Lee, Jinwoo Lee, Weontae Lee, Bernard Brooks, Sung Jong Lee, Jooyoung Lee
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