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A mitochondria-targeted S -nitrosothiol modulates respiration, nitrosates thiols, and protects against ischemia-reperfusion injury
Open accessAbstract
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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“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]
In the citing paper
“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]
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“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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Targeting Antioxidants to Mitochondria by Conjugation to Lipophilic Cations
Murphy, M. P., & Smith, R. A. J. (2007) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.47.120505.105110 · Cited by 1,173
Self-citationBrown, G. C., & Cooper, C. E. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)01290-3 · Cited by 1,055
Does nitric oxide modulate mitochondrial energy generation and apoptosis?
Moncada, S., & Erusalimsky, J. D. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm762 · Cited by 794
Redox-based regulation of signal transduction: principles, pitfalls, and promises
Janssen-Heininger, Y. M. W., Mossman, B. T., Heintz, N. H., Forman, H. J., Kalyanaraman, B., Finkel, T., Stamler, J. S., Rhee, S. G., & van der Vliet, A. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.011 · Cited by 784
Delivery of bioactive molecules to mitochondria in vivo
Smith, R. A. J., Porteous, C. M., Gane, A. M., & Murphy, M. P. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0931245100 · Cited by 725
Self-citationRedistribution of Intracellular Oxygen in Hypoxia by Nitric Oxide: Effect on HIF1α
Hagen, T., Taylor, C. T., Lam, F., & Moncada, S. (2003) · Science · doi:10.1126/science.1088805 · Cited by 704
Self-citationShiva, S., Sack, M. N., Greer, J. J., Duranski, M., Ringwood, L. A., Burwell, L., Wang, X., MacArthur, P. H., Shoja, A., Raghavachari, N., et al. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20070198 · Cited by 555
Self-citationSubcellular components: preparation and fractionation;
Birnie, G. D. (1972) · Cited by 422
The Biochemistry and Physiology of S-Nitrosothiols
Hogg, N. (2002) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.42.092501.104328 · Cited by 412
Feelisch, M., Rassaf, T., Mnaimneh, S., Singh, N., Bryan, N. S., Jourd'Heuil, D., & Kelm, M. (2002) · The FASEB Journal · doi:10.1096/fj.02-0363com · Cited by 401
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Self-citationKalogeris, T. J., Baines, C. P., Krenz, M., & Korthuis, R. J. (2016) · Comprehensive physiology · doi:10.1002/cphy.c160006 · Cited by 856
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Green, D. R., Galluzzi, L., & Kroemer, G. (2014) · Science · doi:10.1126/science.1250256 · Cited by 678
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Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588
Smith, R. A. J., Hartley, R. C., Cochemé, H. M., & Murphy, M. P. (2012) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2012.03.010 · Cited by 514
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Lima, B., Forrester, M. T., Hess, D. T., & Stamler, J. S. (2010) · Circulation Research · doi:10.1161/circresaha.109.207381 · Cited by 490
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Murphy, E., Ardehali, H., Balaban, R. S., Lisa, F. D., Dorn, G. W., Kitsis, R. N., Otsu, K., Ping, P., Rizzuto, R., Sack, M. N., et al. (2016) · Circulation Research · doi:10.1161/res.0000000000000104 · Cited by 476
Figueira, T. R., de Barros, M. H., Camargo, A. A., Castilho, R. F., Ferreira, J. C. B., Kowaltowski, A. J., Sluse, F. E., de Souza-Pinto, N. C., & Vercesi, A. E. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4729 · Cited by 430
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Synergy effects of herb extracts: Pharmacokinetics and pharmacodynamic basis
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Mitochondrial-targeted fluorescent probes for reactive oxygen species
Dickinson, B. C., Srikun, D., & Chang, C. J. (2009) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2009.10.014 · Cited by 318
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Gould, N., Doulias, P.-T., Tenopoulou, M., Raju, K., & Ischiropoulos, H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.460261 · Cited by 274
Mitochondria as a Drug Target in Ischemic Heart Disease and Cardiomyopathy
Walters, A. M., Porter, G. A., & Brookes, P. S. (2012) · Circulation Research · doi:10.1161/circresaha.112.265660 · Cited by 272
Self-citationMitochondria as a therapeutic target for ischemic stroke
He, Z., Ning, N., Zhou, Q., Khoshnam, S. E., & Farzaneh, M. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.11.005 · Cited by 272
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de Groot, P. C. E., Thijssen, D. H. J., Sanchez, M., Ellenkamp, R., & Hopman, M. T. E. (2009) · European Journal of Applied Physiology · doi:10.1007/s00421-009-1195-2 · Cited by 260
Mitochondrial redox signalling at a glance
Collins, Y., Chouchani, E. T., James, A. M., Menger, K. E., Cochemé, H. M., & Murphy, M. P. (2012) · Journal of Cell Science · doi:10.1242/jcs.098475 · Cited by 264
Self-citationDoulias, P.-T., Tenopoulou, M., Greene, J. L., Raju, K., & Ischiropoulos, H. (2013) · Science Signaling · doi:10.1126/scisignal.2003252 · Cited by 250
Levonen, A., Hill, B. G., Kansanen, E., Zhang, J., & Darley-Usmar, V. M. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.025 · Cited by 235
Requejo, R., Hurd, T. R., Costa, N. J., & Murphy, M. P. (2010) · The FEBS Journal · doi:10.1111/j.1742-4658.2010.07576.x · Cited by 231
Self-citationProtein S -Nitrosylation and Cardioprotection
Sun, J., & Murphy, E. (2010) · Circulation Research · doi:10.1161/circresaha.109.209452 · Cited by 205
Penna, C. R. R., Perrelli, M.-G., & Pagliaro, P. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4459 · Cited by 182
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Guo, X., Xiao, W., Chen, Z., Zhang, X., Yang, G., & Zhou, S. (2019) · Progress in Materials Science · doi:10.1016/j.pmatsci.2019.100599 · Cited by 171
van Golen, R. F., Reiniers, M. J., Olthof, P. B., van Gulik, T. M., & Heger, M. (2012) · Journal of Gastroenterology and Hepatology · doi:10.1111/jgh.12072 · Cited by 165
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Tullio, F., Angotti, C., Perrelli, M.-G., Penna, C. R. R., & Pagliaro, P. (2013) · Basic Research in Cardiology · doi:10.1007/s00395-013-0392-7 · Cited by 152
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Jean, S. R., Tulumello, D. V., Wisnovsky, S., Lei, E. K., Pereira, M. P., & Kelley, S. O. (2014) · ACS Chemical Biology · doi:10.1021/cb400821p · Cited by 150
Neurological deficits caused by tissue hypoxia in neuroinflammatory disease
Davies, A. L., Desai, R. A., Bloomfield, P. S., McIntosh, P. R., Chapple, K. J., Linington, C., Fairless, R., Diem, R., Kasti, M., Murphy, M. P., et al. (2013) · Annals of Neurology · doi:10.1002/ana.24006 · Cited by 142
Self-citationVercesi, A. E., Castilho, R. F., Kowaltowski, A. J., Oliveira, H. C. F., de Souza-Pinto, N. C., Figueira, T. R., & Busanello, E. N. B. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.08.034 · Cited by 146
Chouchani, E. T., Hurd, T. R., Nadtochiy, S. M., Brookes, P. S., Fearnley, I. M., Lilley, K. S., Smith, R. A. J., & Murphy, M. P. (2010) · Biochemical Journal · doi:10.1042/bj20100633 · Cited by 137
Self-citationStructural basis for a complex I mutation that blocks pathological ROS production
Yin, Z., Burger, N., Kula‐Alwar, D., Aksentijević, D., Bridges, H. R., Prag, H. A., Grba, D. N., Viscomi, C. F., James, A. M., Mottahedin, A., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-20942-w · Cited by 132
Self-citationLack of Oxygen Deactivates Mitochondrial Complex I
Galkin, A. S., Abramov, A. Y., Frakich, N., Duchen, M. R., & Moncada, S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.054346 · Cited by 132
Lysine deacetylation in ischaemic preconditioning: the role of SIRT1
Nadtochiy, S. M., Redman, E., Rahman, I., & Brookes, P. S. (2011) · Cardiovascular Research · doi:10.1093/cvr/cvq287 · Cited by 130
Self-citationThe Key Role of Nitric Oxide in Hypoxia: Hypoxic Vasodilation and Energy Supply–Demand Matching
Umbrello, M., Dyson, A., Feelisch, M., & Singer, M. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4979 · Cited by 138
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Zhao, X., Lu, M., Yuan, D., Xu, D.-E., Yao, P.-P., Ji, W., Chen, H., Liu, W., Yan, C.-X., Xia, Y., et al. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00030 · Cited by 132
Nitrosative Stress and Its Association with Cardiometabolic Disorders
Pérez-Torres, I., Manzano-Pech, L., Rubio-Ruiz, M. E., Soto, M. E., & Guarner‐Lans, V. (2020) · Molecules · doi:10.3390/molecules25112555 · Cited by 129
Nadtochiy, S. M., & Redman, E. (2011) · Nutrition · doi:10.1016/j.nut.2010.12.006 · Cited by 125
Self-citationPorteous, C. M., Logan, A., Evans, C., Ledgerwood, E. C., Menon, D. K., Aigbirhio, F., Smith, R. A. J., & Murphy, M. P. (2010) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2010.06.001 · Cited by 121
Self-citationPagliaro, P., Moro, F., Tullio, F., Perrelli, M.-G., & Penna, C. R. R. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3245 · Cited by 122
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Huang, Z. M., Gao, E., Fonseca, F. V., Hayashi, H., Shang, X., Hoffman, N. E., Chuprun, J. K., Tian, X., Tilley, D. G., Madesh, M., et al. (2013) · Science Signaling · doi:10.1126/scisignal.2004225 · Cited by 107
Proteomic approaches to the characterization of protein thiol modification
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Self-citationKarwi, Q. G., Bornbaum, J., Boengler, K., Torregrossa, R., Whiteman, M., Wood, M. E., Schulz, R., & Baxter, G. F. (2016) · British Journal of Pharmacology · doi:10.1111/bph.13688 · Cited by 102
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Wang, J., Li, J. Q., Xiao, Y., Fu, B., & Qin, Z. (2020) · ChemMedChem · doi:10.1002/cmdc.201900695 · Cited by 103
Jara, J. A., Castro-Castillo, V., Saavedra‐Olavarría, J., Peredo-Silva, L., Pavani, M., Jaña, F., Letelier, M. E., Parra, E., Becker, M. I., Morello, A., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm500174v · Cited by 97
Cardioprotective activity of iron oxide nanoparticles
Xiong, F., Wang, H., Feng, Y., Li, Y., Hua, X., Pang, X., Zhang, S., Song, L., Zhang, Y., & Gu, N. (2015) · Scientific Reports · doi:10.1038/srep08579 · Cited by 94
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Shiva, S. (2010) · Nitric Oxide · doi:10.1016/j.niox.2009.09.002 · Cited by 87
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Kloner, R. A., Brown, D. A., CSETE, M. E., Dai, W., Downey, J. M., Gottlieb, R. A., Hale, S. L., & Shi, J. (2017) · Nature Reviews Cardiology · doi:10.1038/nrcardio.2017.102 · Cited by 86
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Roberts, P. G., & Hirst, J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.384560 · Cited by 87
Selective Inhibition of Deactivated Mitochondrial Complex I by Biguanides
Matsuzaki, S., & Humphries, K. M. (2015) · Biochemistry · doi:10.1021/bi501473h · Cited by 81
Ortiz, F., García, J. A. G., Acuña-Castroviejo, D., Doerrier, C., López, A., Venegas, C., Volt, H., Luna‐Sánchez, M., López, L. C., & Escames, G. (2013) · Journal of Pineal Research · doi:10.1111/jpi.12099 · Cited by 81
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Liu, P., Wang, Y., Liu, Y., Tan, F., Li, J., & Li, N. (2020) · Theranostics · doi:10.7150/thno.42661 · Cited by 76
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Pagliaro, P., & Penna, C. R. R. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12975 · Cited by 75
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Leucker, T. M., Bienengraeber, M., Muravyeva, M., Baotić, I., Weihrauch, D., Brzezinska, A. K., Warltier, D. C., Kersten, J. R., & Pratt, P. F. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2011.06.026 · Cited by 72
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Wang, J., Li, J., Xiao, Y., Fu, B., & Qin, Z. (2020) · RSC Medicinal Chemistry · doi:10.1039/c9md00572b · Cited by 72
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Bazhin, A. A., Sinisi, R., Marchi, U. D., Hermant, A., Sambiagio, N., Maric, T., Budin, G., & Goun, E. A. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0602-1 · Cited by 71
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Yamakoshi, H., Palonpon, A. F., Dodo, K., Ando, J., Kawata, S., Fujita, K., & Sodeoka, M. (2014) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2014.11.080 · Cited by 67
Sokolov, E. P., Markert, S., Hinzke, T., Hirschfeld, C., Becher, D., Ponsuksili, S., & Sokolova, I. M. (2018) · Journal of Proteomics · doi:10.1016/j.jprot.2018.12.009 · Cited by 67
Finichiu, P. G., James, A. M., Larsen, L., Smith, R. A. J., & Murphy, M. P. (2012) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-012-9493-5 · Cited by 65
Self-citationMitochondrial proteome research: the road ahead
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Metadata
- 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 (medical) › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Cardiology and Cardiovascular 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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