2014
DOI: 10.1016/j.freeradbiomed.2014.04.024
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Reevaluation of the rate constants for the reaction of hypochlorous acid (HOCl) with cysteine, methionine, and peptide derivatives using a new competition kinetic approach

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Cited by 139 publications
(123 citation statements)
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“…The main targets for HOCl in proteins are sulfur-containing amino acid residues. Recently reevaluated rate constants of the reaction of HOCl with free cysteine (Cys) and methionine (Met) at pH 7.4 are 3.6 × 10 8 and 3.4 × 10 7 M −1 s −1 , respectively [36]. At higher HOCl concentrations also histidine (His), tryptophan (Trp), and lysine (Lys) residues, as well as ␣-amino groups of terminal amino acids should be regarded as significant targets for HOCl [37].…”
Section: Discussionmentioning
confidence: 99%
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“…The main targets for HOCl in proteins are sulfur-containing amino acid residues. Recently reevaluated rate constants of the reaction of HOCl with free cysteine (Cys) and methionine (Met) at pH 7.4 are 3.6 × 10 8 and 3.4 × 10 7 M −1 s −1 , respectively [36]. At higher HOCl concentrations also histidine (His), tryptophan (Trp), and lysine (Lys) residues, as well as ␣-amino groups of terminal amino acids should be regarded as significant targets for HOCl [37].…”
Section: Discussionmentioning
confidence: 99%
“…Taking into account that heme groups in catalase molecule are deeply buried [3], it is likely that amino acid residues on the protein surface are indeed the main targets for hypochlorous acid. It is well established that oxidizing/chlorinating power of HOCl is much higher than that of OCl − [38,39], whereas cysteine and histidine are much more reactive in their deprotonated form [36,37]. It should be noted that pK a values of cysteine and histidine residues in a protein environment may differ from those of free Cys and His (8.3 and 6.0, respectively).…”
Section: Discussionmentioning
confidence: 99%
“…Selenium compounds have demonstrated high reactivity towards MPO-derived oxidants, with rate constants that are greater than those reported for the analogous sulfur containing compounds [23,24,26]. For example, selenomethionine (SeMet) and 1,4-anhydro-4-seleno-D-talitol (SeTal) react with HOCl with second-order rate constants >10 8 M -1 s -1 , comparable to the second-order rate constants for reaction of HOCl with GSH and Cys [7,27]. In addition, ebselen and SeMet, both selenoethers, have demonstrated ability to detoxify peroxides and peroxynitrous acid, forming an oxidized 7 selenium compound, which can be reduced by GSH, giving a catalytic scavenging cycle analogous to that of glutathione peroxidase (GPx) [28][29][30].…”
Section: Myeloperoxidase (Mpo) Is An Enzyme Released By Neutrophils Amentioning
confidence: 96%
“…HOCl reacts particularly rapidly with sulfur-containing residues (thiols and thioethers), with rate constants in the order of 10 7 -10 8 M -1 s -1 [6,7], making them some of the fastest and most significant reactions for HOCl in most biological systems. As such, intracellular reduced glutathione (GSH) and proteins containing thiol (Cys) residues are maBor targets of HOCl in biological systems.…”
Section: Myeloperoxidase (Mpo) Is An Enzyme Released By Neutrophils Amentioning
confidence: 99%
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