The DOI matches its Crossref record.
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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]
Citations
Cites
Still being checked.
Cited by
Sorted by citations
Free Radicals: Properties, Sources, Targets, and Their Implication in Various Diseases
Phaniendra, A., Jestadi, D. B., & Periyasamy, L. (2015) · Indian Journal of Clinical Biochemistry · doi:10.1007/s12291-014-0446-0 · Cited by 2,886
Deborde, M., & von Gunten, U. (2007) · Water Research · doi:10.1016/j.watres.2007.07.025 · Cited by 2,124
Thiol chemistry and specificity in redox signaling
Winterbourn, C. C., & Hampton, M. B. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.05.004 · Cited by 1,226
The chemistry and biological activities of N-acetylcysteine
Samuni, Y., Goldstein, S., Dean, O. M., & Berk, M. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.04.016 · Cited by 876
Sharma, V. K., Johnson, N. M., Cizmas, L. H., McDonald, T. J., & Kim, H. (2016) · Chemosphere · doi:10.1016/j.chemosphere.2015.12.084 · Cited by 728
Free Radical Properties, Source and Targets, Antioxidant Consumption and Health
Martemucci, G., Costagliola, C., Mariano, M., D’Andrea, L., Napolitano, P., & D‘Alessandro, A. G. (2022) · Oxygen · doi:10.3390/oxygen2020006 · Cited by 854
Occurrence and removal of pharmaceuticals and hormones through drinking water treatment
Huerta‐Fontela, M., Galceran, M. T., & Ventura, F. (2010) · Water Research · doi:10.1016/j.watres.2010.10.036 · Cited by 687
Hypochlorite-induced oxidation of amino acids, peptides and proteins
Hawkins, C. L., Pattison, D. I., & Davies, M. J. (2003) · Amino Acids · doi:10.1007/s00726-003-0016-x · Cited by 600
Mammalian Heme Peroxidases: From Molecular Mechanisms to Health Implications
Davies, M. J., Hawkins, C. L., Pattison, D. I., & Rees, M. D. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1927 · Cited by 559
Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation
Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541
Dodd, M. C. (2012) · Journal of Environmental Monitoring · doi:10.1039/c2em00006g · Cited by 477
Sulfenic acid chemistry, detection and cellular lifetime
Gupta, V., & Carroll, K. S. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.05.040 · Cited by 434
Winterbourn, C. C. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.05.004 · Cited by 429
Myeloperoxidase-derived oxidation: Mechanisms of biological damage and its prevention
Davies, M. J. (2010) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.11-006fr · Cited by 412
Virus Inactivation Mechanisms: Impact of Disinfectants on Virus Function and Structural Integrity
Wigginton, K. R., Pecson, B. M., Sigstam, T., Bosshard, F., & Kohn, T. (2012) · Environmental Science & Technology · doi:10.1021/es3029473 · Cited by 417
Biomarkers of myeloperoxidase-derived hypochlorous acid
Winterbourn, C. C., & Kettle, A. J. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00204-5 · Cited by 390
Peskin, A. V., & Winterbourn, C. C. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00506-2 · Cited by 335
The Role of Myeloperoxidase in Biomolecule Modification, Chronic Inflammation, and Disease
Davies, M. J., & Hawkins, C. L. (2020) · Antioxidants & Redox Signaling · doi:10.1089/ars.2020.8030 · Cited by 332
Polyphenol composition, vitamin C content and antioxidant capacity of Mauritian citrus fruit pulps
Ramful‐Baboolall, D., Tarnus, E., Aruoma, O. I., Bourdon, E., & Bahorun, T. (2011) · Food Research International · doi:10.1016/j.foodres.2011.03.056 · Cited by 317
Living with a Killer: The Effects of Hypochlorous Acid on Mammalian Cells
Pullar, J. M., Vissers, M. C. M., & Winterbourn, C. C. (2000) · IUBMB Life · doi:10.1080/713803731 · Cited by 316
Hawkins, C. L., & Davies, M. J. (1998) · Biochemical Journal · doi:10.1042/bj3320617 · Cited by 305
Bacterial Responses to Reactive Chlorine Species
Gray, M. J., Wholey, W.-Y., & Jakob, U. (2013) · Annual Review of Microbiology · doi:10.1146/annurev-micro-102912-142520 · Cited by 303
RNA under attack: Cellular handling of RNA damage
Wurtmann, E. J., & Wolin, S. L. (2008) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230802594043 · Cited by 275
Chen, S., Chen, H., Du, Q., & Shen, J. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00433 · Cited by 290
Yoon, Y., Chung, H. J., Di, D. Y. W., Dodd, M. C., Hur, H., & Lee, Y. (2017) · Water Research · doi:10.1016/j.watres.2017.06.056 · Cited by 267
The Roles of Neutrophil-Derived Myeloperoxidase (MPO) in Diseases: The New Progress
Lin, W. C., Chen, H., Chen, X., & Guo, C. (2024) · Antioxidants · doi:10.3390/antiox13010132 · Cited by 290
Malle, E., Waeg, G., Schreiber, R., Gröne, E. F., Sattler, W., & Gröne, H. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01498.x · Cited by 245
Oxidant-induced apoptosis is mediated by oxidation of the actin-regulatory protein cofilin
Klamt, F., Zdanov, S., Levine, R. L., Pariser, A. C., Zhang, Y., Zhang, B., Yu, L., Veenstra, T. D., & Shacter, E. B. (2009) · Nature Cell Biology · doi:10.1038/ncb1968 · Cited by 241
Oxidative Stress in COPD: Sources, Markers, and Potential Mechanisms
McGuinness, A., & Sapey, E. (2017) · Journal of Clinical Medicine · doi:10.3390/jcm6020021 · Cited by 243
Ulfig, A., & Leichert, L. I. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03591-y · Cited by 239
Myeloperoxidase: A new player in autoimmunity
Strzępa, A., Pritchard, K. A., & Dittel, B. N. (2017) · Cellular Immunology · doi:10.1016/j.cellimm.2017.05.002 · Cited by 244
Bond, T., Goslan, E. H., Parsons, S. A., & Jefferson, B. (2012) · Environmental Technology Reviews · doi:10.1080/09593330.2012.705895 · Cited by 240
He, H., Zhou, P., Shimabuku, K. K., Fang, X., Li, S., Lee, Y., & Dodd, M. C. (2019) · Environmental Science & Technology · doi:10.1021/acs.est.8b04393 · Cited by 227
Resolution of inflammation: Mechanisms and opportunity for drug development
Alessandri, A. L., Sousa, L. P., Lucas, C. D., Rossi, A. G., Pinho, V., & Teixeira, M. M. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.04.006 · Cited by 219
Waterborne Viruses: A Barrier to Safe Drinking Water
Gall, A. M., Mariñas, B. J., Lu, Y., & Shisler, J. L. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004867 · Cited by 210
Wang, L., Ye, C., Guo, L., Chen, C., Kong, X., Chen, Y.-Q., Shu, L., Wang, P., Yu, X., & Fang, J. (2021) · Environmental Science & Technology · doi:10.1021/acs.est.1c00645 · Cited by 201
The physiological role of reversible methionine oxidation
Drazic, A., & Winter, J. (2014) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.01.001 · Cited by 198
Protein Quality Control under Oxidative Stress Conditions
Dahl, J., Gray, M. J., & Jakob, U. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.02.014 · Cited by 206
Oxidative release of natural glycans for functional glycomics
Song, X., Ju, H., Lasanajak, Y., Kudelka, M. R., Smith, D. F., & Cummings, R. D. (2016) · Nature Methods · doi:10.1038/nmeth.3861 · Cited by 191
Hawkins, C. L., & Davies, M. J. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.07.007 · Cited by 184
Virus disinfection mechanisms: the role of virus composition, structure, and function
Wigginton, K. R., & Kohn, T. (2011) · Current Opinion in Virology · doi:10.1016/j.coviro.2011.11.003 · Cited by 176
Pattison, D. I., Davies, M. J., & Hawkins, C. L. (2012) · Free Radical Research · doi:10.3109/10715762.2012.667566 · Cited by 183
Andrés, C. M. C., Pérez de la Lastra, J. M., Juan, C. A., Plou, F. J., & Pérez-Lebeña, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231810735 · Cited by 166
Storkey, C., Davies, M. J., & Pattison, D. I. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.04.024 · Cited by 165
Dalle‐Donne, I., Rossi, R., Giustarini, D., Gagliano, N., Lusini, L., Milzani, A., Simplicio, P. D., & Colombo, R. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00690-6 · Cited by 161
Observations and impacts of bleach washing on indoor chlorine chemistry
Wong, J. P. S., Carslaw, N., Zhao, R., Zhou, S., & Abbatt, J. P. D. (2017) · Indoor Air · doi:10.1111/ina.12402 · Cited by 161
Hypochlorous acid as a precursor of free radicals in living systems
Panasenko, O. M., Gorudko, I. V., & Av, S. (2013) · Biochemistry (Moscow) · doi:10.1134/s0006297913130075 · Cited by 159
Winterbourn, C. C., & Brennan, S. O. (1997) · Biochemical Journal · doi:10.1042/bj3260087 · Cited by 147
Wu, B. J., Kathir, K., Witting, P. K., Beck, K., Choy, K. J., Li, C., Croft, K. D., Mori, T. A., Tanous, D. J., Adams, M. R., et al. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20052321 · Cited by 145
Miyamoto, S., Martinez, G. R., Rettori, D., Augusto, O., Medeiros, M. H. G., & Di Mascio, P. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508170103 · Cited by 137
The cytoprotective role of taurine in exercise-induced muscle injury
Dawson, R., Biasetti, M., Messina, S. M., & Dominy, J. E. (2002) · Amino Acids · doi:10.1007/s007260200017 · Cited by 136
Organic chloramines in chlorine-based disinfected water systems: A critical review
How, Z. T., Kristiana, I., Busetti, F., Linge, K. L., & Joll, C. A. (2017) · Journal of Environmental Sciences · doi:10.1016/j.jes.2017.05.025 · Cited by 137
Hoenicke, K., Gatermann, R., Hartig, L., Mandix, M., & Otte, S. (2004) · Food Additives & Contaminants · doi:10.1080/02652030410001712484 · Cited by 131
Aqueous chemistry of N-halo-compounds
Armesto, X. L., Canle, M., García, M. V., & Santaballa, J. A. (1998) · Chemical Society Reviews · doi:10.1039/a827453z · Cited by 130
Hydrogen Peroxide Formation by Reaction of Peroxynitrite with HEPES and Related Tertiary Amines
Kirsch, M., Lomonosova, E. E., Korth, H., Sustmann, R., & de GROOT, H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.12716 · Cited by 129
Measuring chlorine bleach in biology and medicine
Kettle, A. J., Albrett, A. M., Chapman, A., Dickerhof, N., Forbes, L. V., Khalilova, I. S., & Turner, R. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.07.004 · Cited by 123
Intervention Technologies for Ensuring Microbiological Safety of Meat: Current and Future Trends
Chen, J. H., Ren, Y., Seow, J., Liu, T., Bang, W., & Yuk, H. (2012) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/j.1541-4337.2011.00177.x · Cited by 124
Prütz, W. A. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0440 · Cited by 121
Self-citationDavies, M. J. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107685 · Cited by 119
Armesto, X. L., Canle, M., Fernández, M. I., García, M. V., & Santaballa, J. A. (2000) · Tetrahedron · doi:10.1016/s0040-4020(99)01066-2 · Cited by 120
Spencer, J. P. E. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00190-8 · Cited by 118
Comparative reactivity of myeloperoxidase-derived oxidants with mammalian cells
Rayner, B. S., Love, D. T., & Hawkins, C. L. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.004 · Cited by 114
Myeloperoxidase: Bridging the gap in neurodegeneration
Ray, R. S., & Katyal, A. (2016) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.06.031 · Cited by 120
Hawkins, C. L., & Davies, M. J. (1998) · Journal of the Chemical Society Perkin Transactions 2 · doi:10.1039/a802949k · Cited by 113
Taurine supplementation decreases oxidative stress in skeletal muscle after eccentric exercise
da Silva, L. A., Silveira, P. C. L., Ronsani, M. M., de Souza, P. S., Scheffer, D. D. L., Vieira, L. C., Benetti, M., de Souza, C. T., & Pinho, R. A. (2010) · Cell Biochemistry and Function · doi:10.1002/cbf.1716 · Cited by 111
Neutrophil Myeloperoxidase: Soldier and Statesman
Prokopowicz, Z. M., Marcinkiewicz, J., Katz, D. R., & Chain, B. (2011) · Archivum Immunologiae et Therapiae Experimentalis · doi:10.1007/s00005-011-0156-8 · Cited by 110
Potent antioxidative activity of lycopene: A potential role in scavenging hypochlorous acid
Pennathur, S., Maitra, D., Byun, J., Sliskovic, I., Abdulhamid, I. B., Saed, G. M., Diamond, M. P., & Abu‐Soud, H. M. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.04.003 · Cited by 110
Marsche, G., Heller, R., Fauler, G., Kovacevic, A., Nuszkowski, A., Graier, W. F., Sattler, W., & Malle, E. (2004) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000148703.43429.25 · Cited by 108
Ceragioli, M., Mols, M., Moezelaar, R., Ghelardi, E., Senesi, S., & Abee, T. (2010) · Applied and Environmental Microbiology · doi:10.1128/aem.03003-09 · Cited by 106
Kim, E., Xiong, Y., Cheng, Y., Wu, H.-C., Liu, Y., Morrow, B., Ben-Yoav, H., Ghodssi, R., Rubloff, G., Shen, J., et al. (2014) · Polymers · doi:10.3390/polym7010001 · Cited by 100
Hydrogen sulphide: A novel physiological inhibitor of LDL atherogenic modification by HOCl
Laggner, H., Muellner, M. K., Schreier, S. M., Sturm, B., Hermann, M., Exner, M., Laggner, H., Muellner, M. K., Schreier, S. M., Sturm, B., et al. (2007) · Free Radical Research · doi:10.1080/10715760701263265 · Cited by 103
Fu, S., Wang, H., Davies, M. J., & Dean, R. T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.15.10851 · Cited by 103
Pullar, J. M., Winterbourn, C. C., & Vissers, M. C. M. (1999) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1999.277.4.h1505 · Cited by 102
REES, M. D., HAWKINS, C. L., & DAVIES, M. J. (2004) · Biochemical Journal · doi:10.1042/bj20040148 · Cited by 100
Peskin, A. V., & Winterbourn, C. C. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.08.019 · Cited by 98
Zhan, Z., Liu, R., Chai, L., Li, Q., Zhang, K., & Lv, Y. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b02613 · Cited by 96
Modified HDL: Biological and physiopathological consequences
Norata, G. D., Pirillo, A., & Catapano, A. L. (2006) · Nutrition Metabolism and Cardiovascular Diseases · doi:10.1016/j.numecd.2006.01.012 · Cited by 96
Vissers, M. C. M., Pullar, J. M., & Hampton, M. B. (1999) · Biochemical Journal · doi:10.1042/bj3440443 · Cited by 95
Rees, M. D., Hawkins, C. L., & Davies, M. J. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0370591 · Cited by 95
Effects of hypochlorous acid on unsaturated phosphatidylcholines
Arnhold, J., Osipov, A. N., Spalteholz, H., Panasenko, O. M., & Schiller, J. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00695-5 · Cited by 95
Renzo, M. D., Ellis, T. H., Sacher, E., & Stangel, I. (2001) · Biomaterials · doi:10.1016/s0142-9612(00)00240-4 · Cited by 91
Chen, C.-Y. O., & Blumberg, J. B. (2008) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf800061z · Cited by 91
Pullar, J. M., Vissers, M. C. M., & Winterbourn, C. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102088200 · Cited by 91
Activation of RidA chaperone function by N-chlorination
Müller, A., Schäkermann, S., Lupilova, N., Kuhlmann, K., Bandow, J. E., & Leichert, L. I. O. (2014) · Nature Communications · doi:10.1038/ncomms6804 · Cited by 85
Ability of Hypochlorous Acid and N-Chloramines to Chlorinate DNA and Its Constituents
Stanley, N., Pattison, D. I., & Hawkins, C. L. (2010) · Chemical Research in Toxicology · doi:10.1021/tx100188b · Cited by 88
Myeloperoxidase-induced Genomic DNA-centered Radicals
Gomez-Mejiba, S., Zhai, Z., Giménez, M. S., Ashby, M. T., Chilakapati, J., Kitchin, K. T., Mason, R. P., & Ramírez, D. C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.086579 · Cited by 85
Kinetics and Mechanisms of Chlorine Dioxide and Chlorite Oxidations of Cysteine and Glutathione
Ison, A., Odeh, I. N., & Margerum, D. W. (2006) · Inorganic Chemistry · doi:10.1021/ic0609554 · Cited by 86
A photoacoustic FTIRS study of the chemical modifications of human dentin surfaces:
Renzo, M. D., Ellis, T. H., Sacher, E., & Stangel, I. (2001) · Biomaterials · doi:10.1016/s0142-9612(00)00239-8 · Cited by 85
Electrodeposition of a Biopolymeric Hydrogel: Potential for One-Step Protein Electroaddressing
Gray, K. M., Liba, B. D., Wang, Y., Cheng, Y., Rubloff, G. W., Bentley, W. E., Montembault, A., Royaud, I., David, L., & Payne, G. F. (2012) · Biomacromolecules · doi:10.1021/bm3001155 · Cited by 84
Neutrophil myeloperoxidase revisited: it's role in health and disease
Deby-Dupont, G. P., Deby, C. M. T., & Lamy, M. (1999) · Intensivmedizin und Notfallmedizin · doi:10.1007/s003900050270 · Cited by 84
Sensitive detection and estimation of cell-derived peroxynitrite fluxes using fluorescein-boronate
Ríos, N., Piacenza, L., Trujillo, M., Martínez, A., Demicheli, V., Prolo, C., Álvarez, M. N., López, G. V., & Radí, R. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.08.033 · Cited by 84
Choi, Y., He, H., Dodd, M. C., & Lee, Y. (2021) · Environmental Science & Technology · doi:10.1021/acs.est.0c05274 · Cited by 85
Chlorinated lipids and fatty acids: An emerging role in pathology
Spickett, C. M. (2007) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2007.06.002 · Cited by 82
Arnhold, J., Osipov, A. N., Spalteholz, H., Panasenko, O. M., & Schiller, J. (2002) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(02)00271-4 · Cited by 82
Oxidation of phosphorothioate DNA modifications leads to lethal genomic instability
Kellner, S. M., DeMott, M. S., Cheng, C. P., Russell, B. S., Cao, B., You, D., & Dedon, P. C. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2407 · Cited by 79
Hung, Y., Waters, B. W., Yemmireddy, V. K., & Huang, C. (2017) · Journal of Integrative Agriculture · doi:10.1016/s2095-3119(17)61798-2 · Cited by 76
Unintended Consequences of Air Cleaning Chemistry
Collins, D. B., & Farmer, D. K. (2021) · Environmental Science & Technology · doi:10.1021/acs.est.1c02582 · Cited by 81
Relative reactivities ofN-chloramines and hypochlorous acid with human plasma constituents
Carr, A. C., Hawkins, C. L., Thomas, S. R., Stocker, R., & Frei, B. B. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00495-0 · Cited by 79
Maiocchi, S. L., Ku, J., Thai, T., Chan, E., Rees, M. D., & Thomas, S. R. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107711 · Cited by 78
Iwao, Y., Nakajou, K., Nagai, R., Kitamura, K., Anraku, M., Maruyama, T., & Otagiri, M. (2008) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00013.2008 · Cited by 74
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
