The DOI matches its Crossref record; 252 of the 254 references it cites were found in a registry or an index.
One- and two-electron oxidation of thiols: mechanisms, kinetics and biological fates
Abstract
The oxidation of biothiols participates not only in the defense against oxidative damage but also in enzymatic catalytic mechanisms and signal transduction processes. Thiols are versatile reductants that react with oxidizing species by one- and two-electron mechanisms, leading to thiyl radicals and sulfenic acids, respectively. These intermediates, depending on the conditions, participate in further reactions that converge on different stable products. Through this review, we will describe the biologically relevant species that are able to perform these oxidations and we will analyze the mechanisms and kinetics of the one- and two-electron reactions. The processes undergone by typical low-molecular-weight thiols as well as the particularities of specific thiol proteins will be described, including the molecular determinants proposed to account for the extraordinary reactivities of peroxidatic thiols. Finally, the main fates of the thiyl radical and sulfenic acid intermediates will be summarized.
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
“Formation of cysteine thiyl radical and sulfenic acid is a reversible process and both intermediates are highly unstable. Both serve as precursors for several oxidized cysteine modifications (Fig. 1A) [16].”
From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [16]
Citations
Cites
Schafer, F. Q., & Buettner, G. R. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00480-4 · Cited by 4,587
Rate Constants for Reactions of Inorganic Radicals in Aqueous Solution
Neta, P., Huie, R. E., & Ross, A. B. (1988) · Journal of Physical and Chemical Reference Data · doi:10.1063/1.555808 · Cited by 3,651
Mitochondrial free radical generation, oxidative stress, and aging
Cadenas, E., & Davies, K. J. A. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00317-8 · Cited by 3,010
Peroxynitrite oxidation of sulfhydryls.
Radí, R., Beckman, J. S., Bush, K., & Freeman, B. Α. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)64313-7 · Cited by 2,492
Myeloperoxidase: friend and foe
Klebanoff, S. J. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.1204697 · Cited by 2,282
Reduction potentials of one-electron couples involving free radicals in aqueous solution
Wardman, P. (1989) · Journal of Physical and Chemical Reference Data · doi:10.1063/1.555843 · Cited by 2,123
The reaction of NO with superoxide
Huie, R. E., & Padmaja, S. (1993) · Free Radical Research Communications · doi:10.3109/10715769309145868 · Cited by 2,121
The chemistry of peroxynitrite: A product from the reaction of nitric oxide with superoxide
Pryor, W. A., & Squadrito, G. L. (1995) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1995.268.5.l699 · Cited by 1,511
Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils
Eiserich, J. P., Hristova, M., Cross, C. E., Jones, A. D., Freeman, B. A., Halliwell, B., & van der Vliet, A. (1998) · Nature · doi:10.1038/34923 · Cited by 1,496
Peroxynitrite, a cloaked oxidant formed by nitric oxide and superoxide
Koppenol, W. H., Moreno, J. J., Pryor, W. A., Ischiropoulos, H., & Beckman, J. S. (1992) · Chemical Research in Toxicology · doi:10.1021/tx00030a017 · Cited by 1,338
Cited by
Sorted by citations
Items 101–142 of 142
New Features of the NO/H2S Cross Talk: A Chemical Basis
Bari, S. E., & Olabe, J. A. (2016) · Signaling and communication in plants · doi:10.1007/978-3-319-40713-5_14 · Cited by 7
Radí, R. (2019) · Nitric Oxide · doi:10.1016/j.niox.2019.03.003 · Cited by 7
Collective adaptability in a replication network of minimal nucleobase sequences
Vela-Gallego, S., Pardo-Botero, Z., Moya, C., & de la Escosura, A. (2022) · Chemical Science · doi:10.1039/d2sc02419e · Cited by 6
Antioxidant properties of α-amino acids: a density functional theory viewpoint
Buglak, A. A. (2024) · Free Radical Research · doi:10.1080/10715762.2024.2385338 · Cited by 6
Equipping Coiled-Coil Peptide Dimers With Furan Warheads Reveals Novel Cross-Link Partners
Miret‐Casals, L., Putte, S. V. D., Aerssens, D., Diharce, J., Bonnet, P., & Madder, A. (2022) · Frontiers in Chemistry · doi:10.3389/fchem.2021.799706 · Cited by 6
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
Gao, Q., Grzyb, K., Gamon, L. F., Ogilby, P. R., Pędziński, T., & Davies, M. J. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.08.024 · Cited by 6
Sieber, P. H., Steinritz, D., Worek, F., & John, H. (2024) · Analytical Biochemistry · doi:10.1016/j.ab.2024.115568 · Cited by 6
Santos, A. C. F., Moura, F. A., Tanaka, A. A., Luz, R. D. C. S., Damos, F. S., Kubota, L. T., & Goulart, M. O. F. (2016) · Electroanalysis · doi:10.1002/elan.201600205 · Cited by 6
Zhao, N., Song, Z., Zhang, X., Shi, X., Wang, L., Chen, Z., Huang, J., & Wang, X. (2025) · Food Chemistry · doi:10.1016/j.foodchem.2025.142811 · Cited by 5
Dereven’kov, I. А., Tsaba, L. V., Pokrovskaya, E. A., & Makarov, S. V. (2018) · Journal of Coordination Chemistry · doi:10.1080/00958972.2018.1515927 · Cited by 5
Observing Confined Local Oxygen‐induced Reversible Thiol/Disulfide Cycle with a Protein Nanopore
Liu, W., Yang, C., Yang, Z., Yu, R., Long, Y., & Ying, Y. (2023) · Angewandte Chemie · doi:10.1002/ange.202304023 · Cited by 5
Sieber, P. H., Steinritz, D., Worek, F., & John, H. (2024) · Drug Testing and Analysis · doi:10.1002/dta.3776 · Cited by 5
Euceda, N., Jahnke, J., Espinal, A., Louis, M. F., Bashkin, E., Roccanova, P., Espaillat, A., Fuentes, G. V., Nieto, F., & Gao, R. (2021) · Physical Chemistry Chemical Physics · doi:10.1039/d1cp00101a · Cited by 7
Vazquez, D. S., Zeida, A., Agudelo, W. A., Montes, M. R., Ferrer‐Sueta, G., & Santos, J. (2020) · Physical Chemistry Chemical Physics · doi:10.1039/d0cp00140f · Cited by 5
Special issue on “Free Radical and Redox Biochemistry of Thiols”
Radí, R., & Trujillo, M. (2016) · Free Radical Research · doi:10.3109/10715762.2015.1121254 · Cited by 5
Self-citationElastomeric Silicone Sponges for Bleach Delivery
Zheng, S., & Brook, M. A. (2021) · ACS Applied Polymer Materials · doi:10.1021/acsapm.1c00101 · Cited by 4
Ghazaiean, M., Aliasgharian, A., Karami, H., Ghasemi, M. M., & Darvishi‐Khezri, H. (2024) · Health Science Reports · doi:10.1002/hsr2.70096 · Cited by 4
Wu, L., Li, H., Gu, Y., Shen, Z., Zhou, Y., & Zuo, J. (2025) · Water Research · doi:10.1016/j.watres.2025.123525 · Cited by 4
Ye, H., Cheng, L., Tu, X., Wang, D.-W., & Yi, L. (2022) · RSC Chemical Biology · doi:10.1039/d2cb00105e · Cited by 4
Ring Opening and C(ω)‐S Coupling: Nickel‐Mediated Transformation of Alicyclic Alkoxyhydroperoxides
Fomenkov, D. I., Budekhin, R. A., Mulina, O. M., Komarova, O. V., Doronin, M. M., Belyakova, Y. Y., He, L., Yaremenko, I. A., & Terent'ev, A. O. (2025) · European Journal of Organic Chemistry · doi:10.1002/ejoc.202401198 · Cited by 3
Rizzi, V., Cosma, P., Abbattista, R., Fini, P., Agostiano, A., Cataldi, T. R. I., & Losito, I. (2019) · Journal of Mass Spectrometry · doi:10.1002/jms.4343 · Cited by 3
MnSOD serves as the central molecule in adaptive thermogenesis (MnSOD functions as a thermoreceptor)
Zhang, X., Liu, H., & Zhang, D. (2021) · Advances in Redox Research · doi:10.1016/j.arres.2021.100027 · Cited by 3
Human serum albumin-adduct biomarkers to prove human poisoning with methanethiol
Zhang, C., Yang, R., Liu, S., Li, P., & Guo, F. (2025) · Toxicology Letters · doi:10.1016/j.toxlet.2025.111741 · Cited by 2
Protein oxidation in crowded environments
Fuentes-Lemus, E. (2026) · Biochemical Journal · doi:10.1042/bcj20250150 · Cited by 2
Razmara, Z., Rosli, M. M., & Razak, I. A. (2025) · Journal of Inorganic and Organometallic Polymers and Materials · doi:10.1007/s10904-025-03847-9 · Cited by 1
Eom, S., Nguyen, H.-V., Qureshi, A., & Han, S. (2026) · Environmental Science & Technology · doi:10.1021/acs.est.5c15961 · Cited by 1
Detecting Protein Sulfenylation in Cells Exposed to a Toxicant
Wages, P. A. (2017) · Current Protocols in Toxicology · doi:10.1002/cptx.16 · Cited by 1
Carabelly, A. N., Oktiani, B. W., Nurashfia, N., Apriasari, M. L., & Puspitasari, D. (2023) · Berkala Kedokteran · doi:10.20527/jbk.v19i1.15703 · Cited by 1
Estructura y mecanismo de acción de peroxirredoxinas: estudio teórico y experimental
Camacho, Z., & ARI, F. (2015)
Ayad, N. H., Gaballah, H. H., Salem, H. A., Hassan, S. A. E.-H., & Kasem, S. M. (2020) · Asian Journal of Biochemistry Genetics and Molecular Biology · doi:10.9734/ajbgmb/2020/v3i130078
Collectivism in a Replication Network of Minimal Nucleobase SequencesPreprint
Vela, S., Pardo, Z. D., Moya, C., & de la Escosura, A. (2021) · Research Square · doi:10.21203/rs.3.rs-927381/v1
Collective Adaptability in a Replication Network of Minimal Nucleobase SequencesPreprint
Vela, S., Pardo, Z. D., Moya, C., & de la Escosura, A. (2022) · Research Square · doi:10.21203/rs.3.rs-927381/v2
Collective Adaptability in a Replication Network of Minimal Nucleobase SequencesPreprint
Vela, S., Pardo, Z. D., Moya, C., & de la Escosura, A. (2022) · Research Square · doi:10.21203/rs.3.rs-927381/v3
Enhancement of Antioxidant Activity of Isorosmanol in Aqueous Micellar Solution by a Cysteine Thiol
Hamasaki, T., & Masuda, T. (2025) · ACS Food Science & Technology · doi:10.1021/acsfoodscitech.5c00619
Jiang, C., Tian, H., Li, E., Zhang, H., Li, Z. C., Shi, T., Liu, Z., & Huo, S. (2025) · Results in Chemistry · doi:10.1016/j.rechem.2025.102972
Yang, X., Chang, H., Graf, A., Li, X. C., Xia, Y., Tahir, A. A., & Zhu, Y. (2026) · ACS Applied Energy Materials · doi:10.1021/acsaem.5c03482
Redox-modulated therapeutics in plasma biomedicine: From chemical reactivity to clinical potential
Park, B., Tamang, S., Rethinasabapathy, M., Kim, B., Han, S., Kim, J., Kang, S.-M., & Huh, Y. S. (2026) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2026.217746 · Cited by 1
Gilbert, D. L., Aschbacher‐Smith, L., Migneault, K. Y., Huddleston, D. A., Cecil, K. M., Beebe, D. W., Zhang, B., Ratner, N., & Prada, C. E. (2026) · Pediatric Neurology · doi:10.1016/j.pediatrneurol.2026.04.024
Chan, W., & Vinogradov, A. A. (2026) · RSC Chemical Biology · doi:10.1039/d6cb00161k
Tyrosine nitration modulates superfolder green fluorescent protein
Chavarría, C., Mastrogiovanni, M., Zeida, A., & Souza, J. M. (2026) · Redox Biochemistry and Chemistry · doi:10.1016/j.rbc.2026.100087
Faleke, H. O., Ziskrout, H., Robles, D., & Pappas, D. (2026) · Analytical Methods · doi:10.1039/d6ay01086e
Metadata
- Authors
- Trujillo, M., Alvarez, B., & Radi, R.
- Affiliations
- Universidad de la República de Uruguay (UY)
- Corresponding author
- Trujillo, Madia
- ORCID
- Trujillo, Madia
- Venue
- Free Radical Research
- Publisher
- Informa UK Limited
- Published
- 2015-11-11
- Volume
- 50
- Issue
- 2
- Pages
- 150-171
- ISSN
- 1029-2470 (ISSN-L)
- 1071-5762
- OpenAlex
- W1957064683
- Cited by
- 142
- References
- 254
- Citations by year
- 2026: 8 · 2025: 10 · 2024: 14 · 2023: 10 · 2022: 17 · 2021: 13 · 2020: 13 · 2019: 12 · 2018: 19 · 2017: 14 · 2016: 11 · 2015: 1
- FWCI
- 1.45
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Free Radical Research (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (R01AI095173)
- 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 › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Keywords
- thiol oxidation, one-electron oxidation, two-electron oxidation, thiyl radicals, sulfenic acid, oxidation mechanism, reaction kinetics, thiol proteins, enzyme catalysis, signal transduction, thiol reductants
- MeSH terms
- Animals, Bacteria, Free Radicals, Humans, Kinetics, Oxidation-Reduction, Sulfenic Acids, Sulfhydryl Compounds, Eukaryota
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