The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
Nitric Oxide and Peroxynitrite Interactions with Mitochondria
Abstract
Nitric oxide (*NO) and peroxynitrite (ONOO-) avidly interact with mitochondrial components, leading to a range of biological responses spanning from the modulation of mitochondrial respiration, mitochondrial dysfunction to the signaling of apoptotic cell death. Physiological levels of *NO primarily interact with cytochrome c oxidase, leading to a competitive and reversible inhibition of mitochondrial oxygen uptake. In turn, this leads to alterations in electrochemical gradients, which affect calcium uptake and may regulate processes such as mitochondrial transition pore (MTP) opening and the release of pro-apoptotic proteins. Large or persistent levels of *NO in mitochondria promote mitochondrial oxidant formation. Peroxynitrite formed either extra- or intra-mitochondrially leads to oxidative damage, most notably at complexes I and II of the electron transport chain, ATPase, aconitase and Mn-superoxide dismutase. Mitochondrial scavenging systems for peroxynitrite and peroxynitrite-derived radicals such as carbonate (CO3*-) and nitrogen dioxide radicals (*NO2) include cytochrome c oxidase, glutathione and ubiquinol and serve to partially attenuate the reactions of these oxidants with critical mitochondrial targets. Detection of nitrated mitochondrial proteins in vivo supports the concept that mitochondria constitute central loci of the toxic effects of excess reactive nitrogen species. In this review we will provide an overview of the biochemical mechanisms by which *NO and ONOO- regulate or alter mitochondrial functions.
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Cites
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“Experiments from different groups have clearly established that •NO -mediated inhibition of cytochrome c oxidase in intact mitochondria is competitive to oxygen and reversible (Brown and Cooper, 1994; Cleeter et al., 1994; Takehara et al., 1995; Cassina and Radi, 1996; Poderoso et al., 1996).”
InfluentialAconitase as iron–sulfur protein, enzyme, and iron-regulatory protein
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“dant-sensitive site due to the labile nature of its 4Fe-4S cluster, which readily evolves to 3Fe-4S upon the reaction with various oxidants (Beinert et al., 1996).”
Regulation of mitochondrial respiration by nitric oxide inhibition of cytochrome c oxidase
Brown, G. C. (2001) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00238-3 · Cited by 602
Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide.
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Nitric oxide synthase activity in mitochondria
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Cytochrome c Nitration by Peroxynitrite
Cassina, A. M., Hodara, R., Souza, J. M., Thomson, L., Castro, L., Ischiropoulos, H., Freeman, B. A., & Radi, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m909978199 · Cited by 354 · cited 4×
“Moreover, peroxynitrite promotes cytochrome c release in intact mitochondria (Borutaite et al., 1999) and •NO-mediated apoptosis may be accompanied of release of nitrated cytochrome c (Hortelano et al., 1999; Cassina et al., 2000).”
InfluentialSelf-citationProteomic method identifies proteins nitrated in vivo during inflammatory challenge
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Cited by
Nitric Oxide and Peroxynitrite in Health and Disease
Pacher, P., Beckman, J. S., & Liaudet, L. (2007) · Physiological Reviews · doi:10.1152/physrev.00029.2006 · Cited by 6,390
Mitochondrial formation of reactive oxygen species
Turrens, J. F. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.049478 · Cited by 5,084
Mitochondria and reactive oxygen species
Kowaltowski, A. J., de Souza-Pinto, N. C., Castilho, R. F., & Vercesi, A. E. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.05.004 · Cited by 1,162
Mitochondria-Ros Crosstalk in the Control of Cell Death and Aging
Marchi, S., Giorgi, C., Suski, J. M., Agnoletto, C., Bononi, A., Bonora, M., De Marchi, E., Missiroli, S., Patergnani, S., Poletti, F., et al. (2012) · Journal of Signal Transduction · doi:10.1155/2012/329635 · Cited by 640
Inflammatory Neurodegeneration Mediated by Nitric Oxide, Glutamate, and Mitochondria
Brown, G. C., & Bal-Price, A. (2003) · Molecular Neurobiology · doi:10.1385/mn:27:3:325 · Cited by 461
Metadata
- Authors
- Radi, R., Cassina, A., & Hodara, R.
- Venue
- Biological Chemistry
- Publisher
- Walter de Gruyter GmbH
- Published
- 2002-01-12
- Volume
- 383
- Issue
- 3-4
- Pages
- 401-9
- ISSN
- 1431-6730 (ISSN-L)
- OpenAlex
- W1999098395
- Cited by
- 293
- References
- 16
- FWCI
- 6.16
- Type
- journal article
- Language
- en
- Open access
- closed
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