A mitochondria-targeted S -nitrosothiol modulates respiration, nitrosates thiols, and protects against ischemia-reperfusion injury
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Nitric oxide (NO • ) competitively inhibits oxygen consumption by mitochondria at cytochrome c oxidase and S -nitrosates thiol proteins. We developed mitochondria-targeted S -nitrosothiols (MitoSNOs) that selectively modulate and protect mitochondrial function. The exemplar MitoSNO1, produced by covalently linking an S -nitrosothiol to the lipophilic triphenylphosphonium cation, was rapidly and extensively accumulated within mitochondria, driven by the membrane potential, where it generated NO • and S -nitrosated thiol proteins. MitoSNO1-induced NO • production reversibly inhibited respiration at cytochrome c oxidase and increased extracellular oxygen concentration under hypoxic conditions. MitoSNO1 also caused vasorelaxation due to its NO • generation. Infusion of MitoSNO1 during reperfusion was protective against heart ischemia-reperfusion injury, consistent with a functional modification of mitochondrial proteins, such as complex I, following S -nitrosation. These results support the idea that selectively targeting NO • donors to mitochondria is an effective strategy to reversibly modulate respiration and to protect mitochondria against ischemia-reperfusion injury.
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Prior work showed that complex I is inhibited by various nitric oxide donors in vitro and that this inhibition is associated with S-nitrosation.
“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 [11]
MitoSNO contains an S-nitrosating moiety attached to a lipophilic triphenylphosphonium cation that leads to its rapid and extensive uptake within mitochondria in vivo.
“We used MitoSNO to examine mitochondrial S-nitrosation specifically, as it contains an S-nitrosating moiety attached to a lipophilic triphenylphosphonium cation that leads to its rapid and extensive uptake within mitochondria in vivo11.”
From Cardioprotection by S-nitrosation of a cysteine switch on mitochondrial complex I (2013) · cites this paper as [11]
Pre-ischemic or postischemic use of mitochondrially targeted S-nitrosothiols lessens ischemia-reperfusion injury.
“In separate studies, pre-ischemic (306) or postischemic (336) use of these reagents lessened ischemia-reperfusion injury”
From Redox regulation of mitochondrial function (2012) · cites this paper as [336]
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- Authors
- Prime, T. A., Blaikie, F. H., Evans, C., Nadtochiy, S. M., James, A. M., Dahm, C. C., Vitturi, D. A., Patel, R. P., Hiley, C. R., Abakumova, I., Requejo, R., Chouchani, E. T., Hurd, T. R., Garvey, J. F., Taylor, C. T., Brookes, P. S., Smith, R. A. J., & Murphy, M. P.
- Affiliations
- MRC Mitochondrial Biology Unit (GB)
- University of Otago (NZ)
- University of Rochester Medicine (US)
- Department of Pathology and Center for Free Radical Biology, University of Alabama at Birmingham, 901 19th Street South, Birmingham, AL 35294;
- University of Alabama at Birmingham (US)
- University of Cambridge (GB)
- MRC Mitochondrial Biology Unit, Hills Road, Cambridge CB2 0XY, United Kingdom;
- University College Dublin (IE)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2009-06-30
- Volume
- 106
- Issue
- 26
- Pages
- 10764-10769
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2696550
- OpenAlex
- W2061490621
- Cited by
- 222
- References
- 20
- Citations by year
- 2026: 2 · 2025: 8 · 2024: 7 · 2023: 9 · 2022: 11 · 2021: 8 · 2020: 11 · 2019: 8 · 2018: 11 · 2017: 9 · 2016: 16 · 2015: 11 · 2014: 28 · 2013: 24 · 2012: 18
- FWCI
- 13.03
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- University of Otago
- Health Research Board
- Science Foundation Ireland
- National Institutes of Health
- Medical Research Council
- National Heart, Lung, and Blood Institute (HL-071158, R01HL071158)
- Topics
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Pathology and Forensic Medicine › Cardiac Ischemia and Reperfusion
- Keywords
- nitric oxide, S-nitrosylation, cytochrome c oxidase inhibition, mitochondrial respiration, ischemia-reperfusion injury, heart protection, triphenylphosphonium, membrane potential, hypoxia, vasorelaxation, complex I, mitochondrial proteins
- MeSH terms
- Animals, Aorta, Thoracic, Cell Line, Heart, HeLa Cells, Humans, Male, Mice, Inbred C57BL, Mitochondria, Mitochondria, Heart, Nitric Oxide, Oxygen Consumption, Mass Spectrometry, Sulfhydryl Compounds, Vasodilation, Reperfusion Injury, Nitrosation, Rats, Sprague-Dawley, S-Nitrosothiols, Myoblasts, Electron Transport Complex I, Mice, Rats, Membrane Potential, Mitochondrial, In Vitro Techniques
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