Hypochlorite protein oxidation

HOCl-mediated protein oxidation accelerates under pathophysiological conditions. Thus, proteins from extracellular matrix obtained from advanced human atherosclerotic lesions contained the enhanced levels of oxidized amino acids (DOPA and dityrosine) compared to healthy arterial tissue [44], It was also found that superoxide enhanced the prooxidant effect of hypochlorite in protein oxidation supposedly by the decomposition of chloramines and chlor-amides forming nitrogen-centered free radicals and increasing protein fragmentation [45], In addition to chlorination, hypochlorite is able to oxidize proteins. The most readily oxidized amino acid residue of protein is methionine. Methionine is reversibly oxidized by many oxidants including hypochlorite to methionine sulfide and irreversibly to methionine sulfone [46] ... 

Hawkins CL, Pattison DI, Davies MJ (2003) Hypochlorite-Induced Oxidation of Amino Acids, Peptides and Proteins. Amino Acids 25 259... 

Oxidizing bleaches kill microbes by reacting with cell membranes and cell proteins. The most widely used is sodium hypochlorite for household and hospital uses, and calcium hypochlorite for drinking water and swimming pool disinfecting. 

Alpha-l-antiprotease (ai-AP) limits tissue damage arising from the actions of the leucocyte protease, elastase (Carrell and Travis, 1985), and there is much evidence available for the oxidative inactivation of this protein by oxygen-derived free-radical species and hypochlorous acid/hypochlorite anion (HOCl/OCP). The mechanism of this inactivation appears to involve the oxidation of a critical methionine residue (Met-358) to its corresponding sulphoxide and methionine sulphoxide has been detected in ai-AP samples isolated from the lungs of cigarette smokers (Carp et al., 1982) and rheumatoid synovial fluids (Wong and Travis, 1980). 

Thiols are easily oxidized to disulphides, an important feature of protein structure. Vigorous oxidation with KMn04, HNO3 or sodium hypochlorite (NaOCl) produces sulphonic acids. 

The 2,2,6,6-tetramethylpiperidinoxyl (TEMPO) radical was first prepared in 1960 by Lebedev and Kazarnovskii by oxidation of its piperidine precursor. TEMPO is a highly persistent radical, resistant to air and moisture, which is stabilized primarily by the steric hindrance of the NO-bond. Paramagnetic TEMPO radicals can be used as powerful spin probes for investigating the structure and dynamics of biopolymers such as proteins, DNA, and synthetic polymers by ESR spectroscopy [7]. A versatile redox chemistry has been reported for TEMPO radicals. The radical species can be transformed by two-electron reduction into the respective hydroxyl-amine or by two-electron oxidation into the oxoammonium salt [8]. One-electron oxidations involving oxoammonium salts have also been postulated [9]. The TEMPO radical is usually employed under phase-transfer conditions with, e.g., sodium hypochlorite as activating oxidant in the aqueous phase. In oxidations of primary alcohols carboxylic acids are often formed by over-oxidation, in addition to the de-... 

Proteins, due to the complexity of their chemical structures, undergo oxidative modifications in subsequent stages which depend both on the presence of oxidation-susceptible groups and on steric availability of these groups for oxidant attacks (S25). Some oxidative structural modifications produced in proteins are common in various oxidants. Some modifications, such as chlorinated and nitrated protein derivatives produced in reactions with hypochlorite, peroxynitrite, and nitric dioxide, are specific for the oxidants employed. Certain oxidative protein modifications, such as interchain or intrachain disulfide bond formation or thiolation, are reversible and may be reduced back to the protein native form when oxidative stress is over (Dl). Other changes, such as sulfone formation, chlorination, and nitration, are irreversible and effect protein denaturation and promote its subsequent degradation. 

The other amino acid residue present in proteins that is susceptible to oxidation is the indole moiety of tryptophan (Fig. 11). The reducing potential of tryptophan is considerably less than that of cysteine and methionine, so oxidation of tryptophanyl residues usually does not occur until all exposed thiol residues are oxidized. Also, the spontaneous oxidation of tryptophanyl residues in proteins is much less probable than that of cysteinyl and methionyl residues. Tryptophan residues are the only chromophoric moieties in proteins which can be photooxi-dized to tryptophanyl radicals by solar UV radiation, even by wavelengths as long as 305 nm (B12). Tryptophanyl residues readily react with all reactive oxygen species, hypochlorite, peroxynitrite, and chloramines. Oxidative modifications of other amino acid residues require use of strong oxidants, which eventually are produced in the cells. Detailed mechanisms of action of these oxidants is described in subsequent sections of this chapter. 

Cl, from which hypochlorite is generated, are sufficient to oxidize AuSTm to gold(in). The gold(lll) species are not immunogenic but hkely react with proteins to generate antigenic species and may carry oxidizing equivalents from the site of the oxidative burst to other cells or macromolecules. 

The selection of an aqueous cleaning system is simplified if only water alone, or water and a commodity chemical alone, are used. The cleaning performance can be somewhat predicted based on solubility characteristics (at the appropriate pH) or by consideration of the peptizing performance of alkalinity on protein or the oxidizing action of sodium hypochlorite on denatured protein. In the case of formulated multifunctional cleaning agents, the performance is more... 

Hydrogen peroxide is a substrate for myeloperoxidase, a multisubunit heme protein of M.W. 150,C, present in primary neutrophilic granules. The active prosthetic groups are two hemes covalently attached to the apoen-zyme. This enzyme catalyzes many kinds of oxidation reactions, but oxidation of halide ions to hypohalite ions appears to be the most important. Hypochlorite ion is the principal compound formed, although Br , I, and SCN (a pseudohalide) can also serve as substrates. The reaction catalyzed is... 

Several copolymers and condensates of oxidized starches with polymers have been developed. For example, products of starch dialdehyde condensation with acrylamide were prepared for further copolymerization with various monomers to form resins for coatings, molding powders,585 and materials for immobilization of enzymes, for instance, alpha amylase.586 Hypochlorite-oxidized starches were also reacted with acrylonitrile.507,521 Hypochlorite-oxidized starches were allowed to react with allylated starch dialdehyde,587 polycondensates of ammonia-dimethylamine-epichlorohydrin,588 polycondensates of starch dialdehyde with melamine,589 urea433,541,590 capable of precipitation of tannin591, carboxyamides,411 urea and formaldehyde,592 proteins,524,593,594 polyfyinyl alcohol),595 alkylammonium salts,519,596 alkoxyalkylamines,597... 

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