The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.
Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide
Abstract
The reactivities of glutathione, cysteine, cysteamine, penicillamine, N-acetylcysteine, dithiothreitol and captopril with superoxide generated from xanthine oxidase and hypoxanthine, and with reagent hydrogen peroxide, have been investigated. Rates of thiol loss on adding hydrogen peroxide, and superoxide-dependent thiol loss and oxygen uptake were measured. The relative reactivities of the different thiols with both oxidants were inversely related to the pK of the thiol group, such that at pH 7.4, penicillamine was the most reactive. N-acetylcysteine weakly reactive and no reaction was seen with captopril. For hydrogen peroxide, the calculated rate constants for the reaction with the thiolate anion all fell within the range 18-26 M(-1) s(-1). With superoxide, our results are consistent with each thiol reacting via a short chain that consumes oxygen and regenerates superoxide. Only with some of the thiols, was the consumed oxygen recovered as hydrogen peroxide. Reported values for the rate constant for the reaction of thiols with superoxide vary over four orders of magnitude, with the highest being > 10(5) M(-1) s(-1). Due to the complexity of the chain reaction, no study so far has been able to obtain accurate values and we consider the best estimates to be in the 30 to 1000 M(-1) s(-1) range.
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
“Cystine and Met do not react with superoxide, but N-acetylcysteine and glutathione GSH do [132,133,134], Figure 49.”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [134]
Citations
Cites
Schreck, R., RIEBER, P., & Baeuerle, P. A. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07761.x · Cited by 3,793
Reactivity of HO2/O− 2 radicals in aqueous solution
Bielski, B. H. J., Cabelli, D. E., Arudi, R. L., & Ross, A. B. (1985) · Journal of Physical and Chemical Reference Data · doi:10.1063/1.555739 · Cited by 2,169
Antioxidant and redox regulation of gene transcription
Sen, C. K., & Packer, L. (1996) · The FASEB Journal · doi:10.1096/fasebj.10.7.8635688 · Cited by 1,972
Aruoma, O. I., Halliwell, B. B., Hoey, B. M., & Butler, J. (1989) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(89)90066-x · Cited by 1,774
Wolff, S. P. (1994) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(94)33021-2 · Cited by 1,240
Thornalley, P. J., & Vašák, M. (1985) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(85)90098-6 · Cited by 1,041
Denu, J. M., & Tanner, K. G. (1998) · Biochemistry · doi:10.1021/bi973035t · Cited by 945
Redox Regulation of NF-kappa B Activation
Flohé, L., Brigelius‐Flohé, R., Saliou, C., Traber, M. G., & Packer, L. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00501-1 · Cited by 859
ROLE OF REVERSIBLE OXIDATION-REDUCTION OF ENZYME THIOLS-DISULFIDES IN METABOLIC REGULATION
Ziegler, D. M. (1985) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.54.070185.001513 · Cited by 838
Generation of Superoxide Free Radical during the Autoxidation of Thiols
Misra, H. P. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42810-x · Cited by 556
Research works printed but not linked: 1
- Bielski, B. H. J.; Shiue, G. G. Oxygen free radicals and tissue damage. New York: Excerpta Medica; 1979:43–56.
Cited by
Sorted by citations
Items 801–801 of 801
Probing the Role of Sulfenylation in Redox Regulation of Protein Kinases.
Truong, T. H. (2014) · Deep Blue (University of Michigan)
Metadata
- Authors
- Winterbourn, C. C., & Metodiewa, D.
- Corresponding author
- Winterbourn, Christine C.
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 1999-08
- Volume
- 27
- Issue
- 3-4
- Pages
- 322-328
- ISSN
- 0891-5849 (ISSN-L)
- OpenAlex
- W2056840435
- Cited by
- 799
- References
- 43
- Citations by year
- 2026: 10 · 2025: 24 · 2024: 23 · 2023: 37 · 2022: 28 · 2021: 32 · 2020: 38 · 2019: 43 · 2018: 34 · 2017: 40 · 2016: 43 · 2015: 49 · 2014: 41 · 2013: 48 · 2012: 45
- FWCI
- 3.99
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Health Research Council of New Zealand
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Physical Sciences › Chemistry › Organic Chemistry › Free Radicals and Antioxidants
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Keywords
- thiol oxidation, superoxide, hydrogen peroxide, glutathione, cysteine, cysteamine, D-penicillamine, N-acetylcysteine, dithiothreitol, captopril, xanthine oxidase, thiolate anion, thiol reactivity, thiol pKa, oxygen consumption, chain reaction, rate constants
- MeSH terms
- Acetylcysteine, Angiotensin-Converting Enzyme Inhibitors, Captopril, Cysteamine, Cysteine, Dithiothreitol, Glutathione, Hydrogen Peroxide, Oxygen Consumption, Penicillamine, Sulfhydryl Compounds, Superoxides, Xanthine Oxidase, Reactive Oxygen Species
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
