The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
S-Nitrosation of Mitochondrial Complex I Depends on Its Structural Conformation
Open accessAbstract
Nitric oxide is known to cause persistent inhibition of mitochondrial respiration as a result of S-nitrosation of NADH: ubiquinone oxidoreductase (complex I) (Clementi, E., Brown, G. C., Feelisch, M., and Moncada, S. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 7631-7636). Little is known about whether such nitrosation occurs in physiological conditions and, if so, what are the possible cellular mechanisms. We have now found that the conformational state (active/deactive transition (Vinogradov, A. D. (1998) Biochim. Biophys. Acta 1364, 169-185)) of mitochondrial complex I is an important factor for the interaction of the enzyme with nitrosothiols and peroxynitrite. Only the deactivated, idle form of complex I was susceptible to inhibition by nitrosothiols and peroxynitrite. In contrast, the active form of the enzyme was insensitive to such treatment. Neither form of complex I was inhibited by nitric oxide itself. Our data suggest that the process of active/deactive transition plays an important role in the regulation of complex I activity and cellular respiration by nitric oxide. The implications of this finding for hypoxic or pathophysiological conditions in vivo are discussed.
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“previous work has shown that complex I is inhibited by various nitric oxide donors in vitro and that this inhibition is associated with S-nitrosation2,10,11,21–24.”
From Cardioprotection by S-nitrosation of a cysteine switch on mitochondrial complex I (2013) · cites this paper as [24]
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Metadata
- Authors
- Galkin, A., & Moncada, S.
- Affiliations
- University College London (GB)
- Corresponding author
- Galkin, Alexander
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2007-12
- Volume
- 282
- Issue
- 52
- Pages
- 37448-37453
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2086448760
- Cited by
- 122
- References
- 46
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 1 · 2023: 4 · 2022: 6 · 2021: 6 · 2020: 5 · 2019: 6 · 2018: 7 · 2017: 9 · 2016: 8 · 2015: 8 · 2014: 12 · 2013: 10 · 2012: 6
- FWCI
- 3.05
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Research Explorer (The University of Manchester) (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Research Portal (Queen's University Belfast) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- S-nitrosylation, mitochondrial complex I, nitric oxide, S-nitrosothiols, peroxynitrite, complex I, mitochondrial respiration inhibition, hypoxia
- MeSH terms
- Animals, Hypoxia, Cattle, Mitochondria, Heart, Models, Biological, Molecular Conformation, Multienzyme Complexes, Myocardium, NAD, NADH, NADPH Oxidoreductases, Nitric Oxide, Sulfhydryl Compounds, Superoxides, Time Factors, Oxidative Stress, Peroxynitrous Acid, Electron Transport Complex I
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