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Hypochlorous Acid Interactions with Thiols, Nucleotides, DNA, and Other Biological Substrates
Abstract
HOC1-induced one-electron oxidation of Fe(CN)(6)4- was used as a reference reaction to investigate the stoichiometry of interaction of HOCl with a variety of biological substrates. GSH and GSSG were both found capable of reacting with four and 2-mercaptoethanol with three HOCl molecules. Stopped-flow investigations, with HOCl in excess, indicate that very fast primary reactions of HOCl with GSH and DTPA are followed by slower secondary reactions. In the case of GSH we propose that one HOCl reacts at the terminal alpha-amino-group and three HOCl react at the -SH group to generate the sulfonylchloride GSO2Cl. This assignment is supported by the finding that reaction of HOCl (in excess) with 2-mercaptonaphthalene generates the absorption spectrum of authentic naphthalene-2-sulfonylchloride. NADH reacts with at least two HOCl molecules. A very fast primary reaction of HOCl was followed by a slower secondary reaction at HOCl/NADH > 2, but neither the primary nor the secondary reaction led to NAD+. Stopped-flow investigations of reactions of HOCl with nucleotides indicate that HOCl reacts slowly with the amino-groups of AMP, CMP, and GMP but very fast with the heterocyclic NH-groups of GMP, inosine, and TMP. AMP and CMP promote, but GMP, inosine, and TMP retard HOCl-induced oxidation of Fe(CN)(6)4-. At present we have no convincing evidence, however, that products of interaction of HOCl with nucleotides are capable of one-electron oxidation of Fe(CN)6(-4), with generation of free radical intermediates. HOCl causes slow but very efficient denaturation of native DNA, in our opinion not by oxidative fragmentation, but due to chlorination of amino- and heterocyclic NH-groups of the DNA-bases, which leads to dissociation of the double strand by the loss of hydrogen bonding. HOCl-induced oxidation of Fe(CN)(6)4- is promoted very efficiently by catalytic amounts of Cu2+. Catalysis is explainable by formation of a CuIFeIII(CN)(6)2- complex, with CuI acting as electron donor in a propagating Fenton-like reaction, CuIFeIII(CN)(6)2- +HOCl-->Cu2+ + Fe(CN)(6)3- + Cl- + OH, the rate constant of which was estimated as k = 1.8 x 10(5) M-1 s-1. HOCl is inactivated by Tris, but Hepes promotes HOCl-induced oxidation of Fe(CN)(6)4- very efficiently; this is a warning against application of such buffers in investigations of HOCl- or myeloperoxidase-induced reactions. Anthranilic acid was found to interact with four HOCl molecules to yield highly reactive (unidentified) one-electron oxidants.
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“iNOS and nNOS show higher affinity toward BH4 than for BH2 (around 10-fold in the absence of l-arginine) (6, 514, 753); however, eNOS shows almost identical binding affinities for BH4 and BH2, and it is thus very sensitive to imbalances in the concentrations of BH4 and BH2 (190).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [753]
In the citing paper
“BH4 can be oxidized in vivo by molecular oxygen or ROS to generate dihydrobiopterin (BH2), a pterin very structurally similar to BH4 but unable to support NO synthesis (544, 753, 933).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [753]
In the citing paper
“l-Arginine is also important for the dimerization of NOS (51, 515) and increases BH4 binding affinity (514, 753).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [753]
In the citing paper
“Other pterins are, in general, unable to support NO synthesis in mammalian NOS enzymes, or can only support a NO synthesis rate much slower than BH4 (753).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [753]
In the citing paper
“Nucleic acids are important targets of chlorination stress with possible mutagenic, genotoxic, and cytotoxic outcomes downstream of chemical modification ( Figure 3C ) (39, 100–102).”
From Hypochlorous Acid: From Innate Immune Factor and Environmental Toxicant to Chemopreventive Agent Targeting Solar UV-Induced Skin Cancer (2022) · cites this paper as [39]
In the citing paper
“HOCl, in equilibrium at physiological pH with its anionic form [hypochlorite (OCl−)], may also induce tissue damage at sites of inflammation involving the oxidation and chlorination of biomolecules targeting peptides (e.g. glutathione), proteins, lipids, and nucleic acids (39, 42, 43, 47, 76, 77).”
From Hypochlorous Acid: From Innate Immune Factor and Environmental Toxicant to Chemopreventive Agent Targeting Solar UV-Induced Skin Cancer (2022) · cites this paper as [39]
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Metadata
- Authors
- Prütz, W. A.
- Affiliations
- University of Freiburg (DE)
- Corresponding author
- Prütz, Walter A.
- Venue
- Archives of Biochemistry and Biophysics
- Publisher
- Elsevier BV
- Published
- 1996-08
- Volume
- 332
- Issue
- 1
- Pages
- 110-120
- ISSN
- 0003-9861 (ISSN-L)
- OpenAlex
- W2025549575
- Cited by
- 327
- References
- 0
- Citations by year
- 2026: 7 · 2025: 15 · 2024: 16 · 2023: 17 · 2022: 18 · 2021: 18 · 2020: 17 · 2019: 11 · 2018: 9 · 2017: 15 · 2016: 9 · 2015: 6 · 2014: 8 · 2013: 15 · 2012: 11
- FWCI
- 2.42
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Archives of Biochemistry and Biophysics (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Physical Sciences › Chemistry › Organic Chemistry › Free Radicals and Antioxidants
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- hypochlorous acid, thiol oxidation, glutathione, glutathione disulfide, 2-mercaptoethanol, DTPA, NADH oxidation, nucleotide oxidation, DNA denaturation, copper catalysis, Fenton-like reaction, one-electron oxidation, reaction stoichiometry
- MeSH terms
- Animals, Copper, Disulfides, DNA, Hypochlorous Acid, Iron, Kinetics, Nucleic Acid Denaturation, Nucleotides, Oxidation-Reduction, Sulfhydryl Compounds, Sulfides, In Vitro Techniques
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