One- and two-electron oxidation of thiols: mechanisms, kinetics and biological fates

ProteinS-glutathionylation: from current basics to targeted modifications

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The Mycobacterial Thioredoxin Peroxidase Can Act as a One-cysteine Peroxiredoxin

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Hypothiocyanite

Ashby, M. T. (2012) · Advances in inorganic chemistry · doi:10.1016/b978-0-12-396462-5.00008-8 · Cited by 46

Protein Topology Determines Cysteine Oxidation Fate: The Case of Sulfenyl Amide Formation among Protein Families

Defelipe, L. A., Lanzarotti, E., Gauto, D. F., Marti, M. A., & Turjanski, A. G. (2015) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1004051 · Cited by 46

Compared Reactivities of Trypanothione and Glutathione in Conjugation Reactions.

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Insights into the mechanism of the reaction between hydrogen sulfide and peroxynitrite

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Thiol redox biochemistry: insights from computer simulations

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Reduction of Phenoxyl Radicals by Thioredoxin Results in Selective Oxidation of Its SH-Groups to Disulfides. An Antioxidant Function of Thioredoxin

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Peroxymonocarbonate and Carbonate Radical Displace the Hydroxyl-like Oxidant in the Sod1 Peroxidase Activity under Physiological Conditions

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Hydroperoxide and peroxynitrite reductase activity of poplar thioredoxin-dependent glutathione peroxidase 5: kinetics, catalytic mechanism and oxidative inactivation

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A spectrophotometric assay for chlorine-containing compounds

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The role of superoxide anion radical in the reduction of ferritin iron by xanthine oxidase.

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Redox regulation in anabolic and catabolic processes

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Reactive Sulfur Species: Kinetics and Mechanism of the Hydrolysis of Cysteine Thiosulfinate Ester

Nagy, P., & Ashby, M. T. (2007) · Chemical Research in Toxicology · doi:10.1021/tx700168z · Cited by 41

Voltammetric investigation of the interactions between superoxide ion and some sulfur amino acids

Feroci, G., & Fini, A. (2006) · Inorganica Chimica Acta · doi:10.1016/j.ica.2006.07.113 · Cited by 40

Reactive Sulfur Species: Kinetics and Mechanisms of the Reaction of Cysteine Thiosulfinate Ester with Cysteine to Give Cysteine Sulfenic Acid

Nagy, P. I., Lemma, K., & Ashby, M. T. (2007) · The Journal of Organic Chemistry · doi:10.1021/jo701813f · Cited by 40

Vascular peroxidase 1 catalyzes the formation of hypohalous acids: Characterization of its substrate specificity and enzymatic properties

Li, H., Cao, Z., Zhang, G., Thannickal, V. J., & Cheng, G. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.08.597 · Cited by 40

Mechanism of the antioxidant action of dialkyl sulfoxides

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Radical-Induced Cis–Trans Isomerization of Fatty Acids: A Theoretical Study

Tzeng, Y.-Z., & Hu, C. (2014) · The Journal of Physical Chemistry A · doi:10.1021/jp502434t · Cited by 39

Peroxynitrite efficiently mediates the interconversion of redox intermediates of myeloperoxidase

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Oxidation of 2-Cys Peroxiredoxins in Human Endothelial Cells by Hydrogen Peroxide, Hypochlorous Acid, and Chloramines

Stacey, M. M., Vissers, M. C. M., & Winterbourn, C. C. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4348 · Cited by 39

A cysteine residue near the propionate side chain of heme is the radical site in ascorbate peroxidase

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Broad specificity AhpC-like peroxiredoxin and its thioredoxin reductant in the sparse antioxidant defense system of Treponema pallidum

Parsonage, D., Desrosiers, D. C., Hazlett, K. R. O., Sun, Y., Nelson, K. J., Cox, D. L., Radolf, J. D., & Poole, L. B. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910057107 · Cited by 38

Redox Properties of Protein Disulfide Bond in Oxidized Thioredoxin and Lysozyme: A Pulse Radiolysis Study

Hanine‐Lmoumene, C. E., Conte, D., Jacquot, J., & Houée‐Levin, C. (2000) · Biochemistry · doi:10.1021/bi000468e · Cited by 36

EPR Detection of Glutathiyl and Hemoglobin-cysteinyl Radicals during the Interaction of Peroxynitrite with Human Erythrocytes

Augusto, O., de Menezes, S. L., Linares, E., Romero, N., Radí, R., & Denicola, A. (2002) · Biochemistry · doi:10.1021/bi0262202 · Cited by 35

Mechanism of Thiol Oxidation by the Superoxide Radical

Cardey, B., Foley, S., & Enescu, M. (2007) · The Journal of Physical Chemistry A · doi:10.1021/jp0731102 · Cited by 35

Chloramines and hypochlorous acid oxidize erythrocyte peroxiredoxin 2

Stacey, M. M., Peskin, A. V., Vissers, M. C. M., & Winterbourn, C. C. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.08.022 · Cited by 35

Mechanism of cysteine oxidation by peroxynitrite: An integrated experimental and theoretical study

Zeida, A., Lebrero, M. C. G., Radí, R., Trujillo, M., & Estrin, D. A. (2013) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2013.08.016 · Cited by 34

Radical Reactions in Aqueous Disulphide-thiol Systems

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Thiol-dependent peroxidases care little about homology-based assignments of function

Flohé, L., Jaeger, T., Pilawa, S., & Sztajer, H. (2003) · Redox Report · doi:10.1179/135100003225002862 · Cited by 33

Extraordinary μs–ms backbone dynamics in Arabidopsis thaliana peroxiredoxin Q

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Protein Radical Formation during Lactoperoxidase-mediated Oxidation of the Suicide Substrate Glutathione

Guo, Q., Detweiler, C. D., & Mason, R. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310034200 · Cited by 31

Mechanisms and Biological Consequences of Peroxynitrite-Dependent Protein Oxidation and Nitration

Trujillo, M., Álvarez, B., Souza, J. M., Romero, N., Castro, L., Thomson, L., & Radí, R. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-373866-0.00003-4 · Cited by 29

Thiyl radical-induced cis/trans -isomerization of methyl linoleate in methanol and of linoleic acid residues in liposomes

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Myeloperoxidase-derived oxidants rapidly oxidize and disrupt zinc–cysteine/histidine clusters in proteins

Cook, N. L., Pattison, D. I., & Davies, M. J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.09.033 · Cited by 26

Mapping the Active Site Helix-to-Strand Conversion of CxxxxC Peroxiredoxin Q Enzymes

Perkins, A., Gretes, M. C., Nelson, K. J., Poole, L. B., & Karplus, P. A. (2012) · Biochemistry · doi:10.1021/bi301017s · Cited by 24

Inhibition of tubulin polymerization by hypochlorous acid and chloramines

Landino, L. M., Hagedorn, T. D., Kim, S. B., & Hogan, K. M. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.01.018 · Cited by 23

Kinetic studies of peroxiredoxin 6 from Arenicola marina: Rapid oxidation by hydrogen peroxide and peroxynitrite but lack of reduction by hydrogen sulfide

Loumaye, E., Ferrer‐Sueta, G., Álvarez, B., Rees, J., Clippe, A., Knoops, B., Radí, R., & Trujillo, M. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.07.002 · Cited by 23

The thermodynamics of thiol sulfenylation

Billiet, L., Geerlings, P., Messens, J., & Roos, G. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.12.029 · Cited by 23

Reactivity toward oxygen radicals and antioxidant action of thiol compounds

Takashima, M., Shichiri, M., Hagihara, Y., Yoshida, Y., & Niki, E. (2012) · BioFactors · doi:10.1002/biof.1014 · Cited by 23

Mechanism of action of the disease-modifying anti-arthritic thiol agents d-penicillamine and sodium aurothiomalate: Restoration of cellular free thiols and sequestration of reactive aldehydes

Wood, P. L., Khan, M. A., & Moskal, J. R. (2007) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2007.10.066 · Cited by 23

Inhibition of protein hydroperoxide formation by protein thiols

Platt, A. A., & Gieseg, S. P. (2003) · Redox Report · doi:10.1179/135100003125001288 · Cited by 23

Hydrogen peroxide targets the cysteine at the active site and irreversibly inactivates creatine kinase

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Cysteine Oxidation by the Superoxide Radical: A Theoretical Study

Cardey, B., & Enescu, M. (2009) · ChemPhysChem · doi:10.1002/cphc.200900010 · Cited by 21

Kinetics of the oxidation of reduced Cu,Zn-superoxide dismutase by peroxymonocarbonate

Ranguelova, K., Ganini, D., Bonini, M. G., London, R. E., & Mason, R. P. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.04.029 · Cited by 21

The formation of a protein sulfenamide during the inactivation of the acyl phosphatase activity of oxidized glyceraldehyde-3-phosphate dehydrogenase by benzylamine

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Garlic: Source of the Ultimate Antioxidants—Sulfenic Acids

Vaidya, V., Ingold, K. U., & Pratt, D. A. (2008) · Angewandte Chemie · doi:10.1002/ange.200804560 · Cited by 20

Protein thiol oxidation and formation of S-glutathionylated cyclophilin A in cells exposed to chloramines and hypochlorous acid

Stacey, M. M., Cuddihy, S. L., Hampton, M. B., & Winterbourn, C. C. (2012) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2012.07.011 · Cited by 17

Electron Capture by the Thiyl Radical and Disulfide Bond: Ligand Effects on the Reduction Potential

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Influence of Intramolecular Electron Transfer Mechanism in Biological Nitration, Nitrosation, and Oxidation of Redox‐Sensitive Amino Acids

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Production of Inflammatory Mediators by Activated C6 Cells Is Attenuated by Taurine Chloramine Inhibition of NF-κB Activation

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How does the protein environment optimize the thermodynamics of thiol sulfenylation? Insights from model systems to QM/MM calculations on human 2-Cys peroxiredoxin

Oláh, J., van Bergen, L., Proft, F. D., & Roos, G. (2014) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2014.907543 · Cited by 8

Oxidative Stress

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Superoxide dismutases: Dual roles in controlling ROS damage and regulating ROS signaling

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Oxygen radicals, nitric oxide, and peroxynitrite: Redox pathways in molecular medicine

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Chemical Biology of H 2 S Signaling through Persulfidation

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Protein oxidation and peroxidation

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Bioactivation of Thiols by One-Electron Oxidation

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Thiol oxidation by biologically-relevant reactive species

Zeida, A., & Radí, R. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-90219-9.00028-5 · Cited by 6

The good and bad sides of thiols as one-electron donors in free radical processes

Schöneich, C. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.07.148

Mechanisms and consequences of protein cysteine oxidation: the role of the initial short-lived intermediates

Turell, L., Zeida, A., & Trujillo, M. (2020) · Essays in Biochemistry · doi:10.1042/ebc20190053 · Cited by 69

Redox Chemistry of Biological Thiols

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