Signaling Functions of Reactive Oxygen Species
Open accessAbstract
We review signaling by reactive oxygen species, which is emerging as a major physiological process. However, among the reactive oxygen species, H(2)O(2) best fulfills the requirements of being a second messenger. Its enzymatic production and degradation, along with the requirements for the oxidation of thiols by H(2)O(2), provide the specificity for time and place that are required in signaling. Both thermodynamic and kinetic considerations suggest that among possible oxidation states of cysteine, formation of sulfenic acid derivatives or disulfides can be relevant as thiol redox switches in signaling. In this work, the general constraints that are required for protein thiol oxidation by H(2)O(2) to be fast enough to be relevant for signaling are discussed in light of the mechanism of oxidation of the catalytic cysteine or selenocysteine in thiol peroxidases. While the nonenzymatic reaction between thiol and H(2)O(2) is, in most cases, too slow to be relevant in signaling, the enzymatic catalysis of thiol oxidation by these peroxidases provides a potential mechanism for redox signaling.
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S-Nitrosation has been implicated as a major player in signal transduction.
“In contrast, S-nitrosation (Eq. 13) has been implicated as a major player in signal transduction [170-173].”
From Signaling and stress: The redox landscape in NOS2 biology (2015) · cites this paper as [173]
Oxidative eustress is characterized by low to mild levels of oxidants involved in the regulation of various biochemical transformations such as carboxylation, hydroxylation, peroxidation, or modulation of signal transduction pathways.
“Oxidative eustress means “good stress” and is characterized by low to mild levels of oxidants involved in the regulation of various biochemical transformations such as carboxylation, hydroxylation, peroxidation, or modulation of signal transduction pathways (Forman et al. 2010).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Forman et al. 2010
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- Authors
- Forman, H. J., Maiorino, M., & Ursini, F.
- Affiliations
- University of California, Merced (US)
- University of Padua (IT)
- Corresponding author
- Forman, Henry Jay
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-01-11
- Volume
- 49
- Issue
- 5
- Pages
- 835-842
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- PMC
- PMC4226395
- OpenAlex
- W2101444644
- Cited by
- 827
- References
- 100
- Citations by year
- 2026: 33 · 2025: 27 · 2024: 42 · 2023: 42 · 2022: 37 · 2021: 36 · 2020: 46 · 2019: 44 · 2018: 35 · 2017: 50 · 2016: 51 · 2015: 65 · 2014: 62 · 2013: 66 · 2012: 82
- FWCI
- 7.19
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Padua Research Archive (University of Padova) (submittedVersion)
- Funders
- National Heart, Lung, and Blood Institute (R01HL037556)
- National Institute of Environmental Health Sciences (ES05511, R56ES005511, R01ES005511)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- reactive oxygen species, hydrogen peroxide, redox signaling, second messengers, thiol oxidation, cysteine oxidation, sulfenic acid, disulfide bond formation, thiol peroxidase, selenocysteine, protein redox regulation
- MeSH terms
- Animals, Cysteine, Humans, Hydrogen Peroxide, Second Messenger Systems, Signal Transduction, Reactive Oxygen Species, Peroxiredoxins
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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.
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