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Nitrite reductase activity is a novel function of mammalian mitochondria
Open accessAbstract
Nitrite, which is the major stable degradation product of nitric oxide, exists in all tissues capable of nitric oxide synthesis from L‐arginine. The present study provides experimental evidence that nitrite in contact with respiring mitochondria accepts reducing equivalents from the ubiquinone cycle of the respiratory chain. Univalent reduction of nitrite was totally inhibited by myxothiazol. We therefore conclude on the involvement of redox cycling that ubisemiquinone is associated with the bc 1 complex. Recycling of nitric oxide degradation products via these electron carriers may become a threat to energy‐linked respiration since nitric oxide in direct contact with mitochondria was shown to slow the energy‐linked respiration down and to trigger a mitochondrial source for superoxide radicals. Until now, the existence of nitrite reductase activity was only demonstrated in plants and bacteria. In addition, the present observation elucidates the existence of a nitric oxide synthase‐independent nitric oxide source.
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“In situations of hypoxia, when the oxygen-dependent NO synthases may become dysfunctional, nitrite reduction is instead greatly enhanced.”
From Nitrate and nitrite in biology, nutrition and therapeutics (2009) · cites this paper as [9]
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“Sruti Shiva (University of Pittsburgh) reviewed a number of studies demonstrating that components of the respiratory chain can reduce nitrite to NO (refs. 4,9)”
From Nitrate and nitrite in biology, nutrition and therapeutics (2009) · cites this paper as [9]
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“This was later confirmed by Kozlov’s group who illustrated that cytochrome c oxidase was an important regulator of nitrite reduction to NO in the mitochondria [120, 121].”
From Inorganic nitrite therapy: historical perspective and future directions (2011) · cites this paper as [120]
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Cites
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Items 201–300 of 341
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The biomolecule ubiquinone exerts a variety of biological functions
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“Beyond hemoglobin, nitrite reduction is catalyzed by other heme-containing globins [myoglobin (86, 193), cytoglobin (126, 174), and neuroglobin (95, 174, 211)], molybdenum metalloenzymes [xanthine oxidoreductase (26, 127), sulfite oxidase (224), and mitochondrial amidoxime-reducing component proteins (200)], NOS (71, 2…”
InfluentialEffect on health from consumption of meat and meat products
Lee, D. Y., Lee, S. Y., Jo, C., Yoon, Y., Jeong, J. Y., & Hur, S. J. (2021) · Journal of Animal Science and Technology · doi:10.5187/jast.2021.e101 · Cited by 20
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A New Paramagnetic Intermediate Formed during the Reaction of Nitrite with Deoxyhemoglobin
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Moderate inhibition of mitochondrial function augments carotid body hypoxic sensitivity
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“NO2 − was selected in this study as (1) it has been shown to release small quantities (nM/pM) of NO at the mitochondria when applied atmillimolar concentrations and (2)NO (and therefore NO2 ) is a rapidly reversible competitive inhibitor of complex IV and thus mitochondrial function [2, 9, 27, 47, 48].”
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Gerdes, H. J., Yang, M., Heisner, J. S., Camara, A. K. S., & Stowe, D. F. (2020) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2020.148290 · Cited by 19
“mitochondrial electron transport chain (ETC) is a source of non-enzymatic NO• production via a nitrate reductase/ubiquinone cycle [40,41].”
Nitric oxide and geriatrics: Implications in diagnostics and treatment of the elderly
Ashley C, T., Mayank, A., & Nathan S, B. (2012) · Journal of Geriatric Cardiology · doi:10.3724/sp.j.1263.2011.00230 · Cited by 101
Bochkova, Z. V., Baizhumanov, A. A., Yusipovich, A. I., Morozova, K. I., Nikelshparg, E. I., Fedotova, A. A., Tiaglik, A. B., Yu, X., Brazhe, A., Maksimov, G. V., et al. (2025) · Biophysical Reviews · doi:10.1007/s12551-025-01270-5 · Cited by 24
“There is overwhelming evidence that mitochondria of many species are capable of reducing nitrite to NO (Kozlov et al. 1999; Tielens et al. 2002; Gupta et al. 2005), which is likely a protective mechanism during hypoxia (Gupta and Igamberdiev 2016).”
Inactivation of nitric oxide by cytochrome c oxidase under steady-state oxygen conditions
Unitt, D. C., Hollis, V. S., Palacios-Callender, M., Frakich, N., & Moncada, S. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.12.002 · Cited by 21
“This is in contrast with studies in which an increase in [NO] at low [O2]was also observed, butwas attributed to the conversion of NO2 − to NO by either cytochrome c oxidase itself [37,38], cytochrome bc1 (mitochondrial complex III) [39,40] or other cytosolic enzymes [41-43] under hypoxic conditions.”
ResultSensing Hypoxia by Mitochondria: A Unifying Hypothesis Involving S-Nitrosation
Ullrich, V., & Schildknecht, S. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4788 · Cited by 19
“It took a while in the scientific community to recognize that such high levels could serve as a source for (cid:2) NO, especially under the strongly reducing conditions found in hypoxic or even anoxic mitochondria (20, 72, 81, 88).”
Vatassery, G. T. (2004) · Neurochemical Research · doi:10.1007/s11064-004-6870-4 · Cited by 18
“Mammalian mitochondria do possess this nitrite reductase activity as shown by Kozlov et al. ( 36 ) and Nohl et al. (30).”
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In Vivo Characterization of a Red Light-Activated Vasodilation: A Photobiomodulation Study
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“Nitrite reductase activity in mammalian tissues has been linked to the mitochondrial electron transport system [104,105], protonation [102], deoxyhemoglobin [106] and xanthine oxidase [107,108].”
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Anaerobic Transcription by OxyR: A Novel Paradigm for Nitrosative Stress
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“More recently, it has been appreciated that mitochondria are also a source of NO, primarily under hypoxic conditions (54), and that S-nitrosothiol (SNO)-based signaling is prevalent within mitochondria.”
BackgroundInfluentialHuman heart mitochondria do not produce physiologically relevant quantities of nitric oxide
Csordás, A., Pankotai, E., Snipes, J. A., Cselenyák, A., Sárszegi, Z., Cziráki, A., Gaszner, B., Papp, L., Benkő, R., Kiss, L., et al. (2006) · Life Sciences · doi:10.1016/j.lfs.2006.10.009 · Cited by 17
Allylic Nitro Compounds as Nitrite Donors
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“In contrast to isoforms of NOS, all of which require L-arginine for NO synthesis, the novel NOS-independent synthase system generates NO from the stable degradation product of this bioregulator synthesized elsewhere in the tissue [57].”
BackgroundFormation of nitric oxide from nitroxyl anion: role of quinones and ferricytochrome c
Büyükafşar, K., Nelli, S., & Martin, W. (2001) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0703812 · Cited by 17
“Nevertheless, since coenzyme Q participates in reactions in mitochondrial complex I (NADH± coenzyme Q reductase), complex II (succinate ± coenzyme Q reductase) and complex III (coenzyme Q ± cytochrome c reductase), we investigated whether the additional presence of the respective cofactor had any e ect on the actions…”
BackgroundInfluentialLow dose nitrite enhances perfusion after fluid resuscitation from hemorrhagic shock
Cabrales, P. (2009) · Resuscitation · doi:10.1016/j.resuscitation.2009.09.005 · Cited by 16
Nitric oxide and dinitrosyl iron complexes: roles in plant iron sensing and metabolism
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Mechanisms of Nitrite Reduction in Ischemia in the Cardiovascular System
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Self-citationTherapeutic Implications of Nitrite in Hypertension
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BackgroundPreserving vessel function during ischemic disease: new possibilities of inorganic nitrite therapy
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Nitric Oxide Formation From Inorganic Nitrate
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“Moreover, we aimed to relate NO2 concentration in striated muscles (as a stable, direct source of NO•) to the muscle content of myoglobin and ETC proteins, which are involved not only in oxygen turnover (oxygen buffering and oxygen usage in OXPHOS) but also in NO• homeostasis [13,17].”
BackgroundInfluentialNitric oxide research in agriculture: bridging the plant and bacterial realms
COHEN, M. F., Mazzola, M., & Yamasaki, H. (2006) · Springer eBooks · doi:10.1007/1-4020-4389-9_5 · Cited by 13
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“enzymes (11), and deoxygenated hemoglobin (4).”
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“While mitochondria and myoglobin have independently been described as nitrite reductase enzymes [22; 28; 31; 36; 39], this study is the first to directly compare the nitrite reduction catalyzed by these two tightly linked functional components of oxygen metabolism, and assess their independent contribution to nitrite-…”
BackgroundResultInfluentialNeither nitrite nor nitric oxide mediate toxic effects of nitroglycerin on mitochondria
Dungel, P., Haindl, S., Behling, T., Mayer, B., Redl, H., & Kozlov, A. V. (2011) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.20389 · Cited by 11
“There are two major hypotheses of how NO can be released from NG: The first suggests that enzymes such as aldehyde dehydrogenase 2 (ALDH2) [1] or cytoplasmic GSH-transferase [2] in a first step release nitrite (NO2 ), which in turn is reduced to NO by mitochondria [3,4]; alternatively, ALDH2 directly releases NO from…”
BackgroundSelf-citationControl of Nitrogen Assimilation in Plants through S-nitrosothiols
Frungillo, L., Spoel, S. H., & Salgado, I. (2016) · Advances in botanical research · doi:10.1016/bs.abr.2015.10.011 · Cited by 11
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“Several studies reported that nitrite-dependent NO formation is critically dependent on the presence of nitrite reductase proteins, including glutathione-S-transferases [20], xanthine oxidoreductase [21], cytochrome P450 enzymes [22], deoxy-Hb and deoxy-myoglobin [23], endothelial NOS [24], and components of the mitoc…”
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“Redox proteins of the mitochondrial electron transport chain, in particular of the COX (Castello et al. 2008), the bc 1 complex (Kozlov et al. 1999), and cytochrome c itself (Basu et al. 2008), can contribute to NO formation from nitrite.”
BackgroundNitrate-Reducing Oral Bacteria: Linking Oral and Systemic Health
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“Although components of the mitochondrial electron transport chain can reduce nitrite to NO, this has only been demonstrated under anaerobic experimental conditions (Brudvig et al. 1980; Kozlov et al. 1999), and not under conditions of physiological oxygen tensions.”
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Effects of Nitrovasodilators on the Human Fetal–Placental Circulation In Vitro
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Higher Plant Mitochondria as a Source for NO
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The Roles and Mechanisms of ROS, Oxidative Stress, and Oxidative Damage
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Nitric Oxide Formation from Inorganic Nitrate and Nitrite
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Impact of mitochondrial nitrite reductase on hemodynamics and myocardial contractility
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Self-citationBringing Nitric Oxide to the Molybdenum World—A Personal Perspective
Maia, L. B. (2023) · Molecules · doi:10.3390/molecules28155819 · Cited by 7
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Impact of mitochondria on nitrite metabolism in HL-1 cardiomyocytes
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“Also mitochondria can rapidly reduce nitrite to NO (Kozlov et al., 1999).”
BackgroundSelf-citationCan Dietary Nitrate Supplements Improve Tolerance to Hypoxia?
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Role of Plant Mitochondria in Nitric Oxide Homeostasis During Oxygen Deficiency
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“The role of the eukaryotic respiratory chain in NO synthesis was initially documented for mammalian mitochondria, in which electron leakage from Complex III (Kozlov et al. 1999) or the nitrite-reducing activity of COX (Castello et al.”
BackgroundENVIRONMENTAL INFLUENCES ON MOSQUITOFISH REPRODUCTION
Edwards, T. M. (2005) · Cited by 7
Simão, S., Santos, D. F., Teixeira, M., Agostinho, R. R., Rodrigues, J., Vitorino, M., & Araújo, I. M. (2025) · Redox Report · doi:10.1080/13510002.2025.2592413 · Cited by 7
“Additional sources of NO include non-enzymatic oxidation of L-Arg [46], xanthine oxidase [47], and other reductases that are able to convert nitrates to nitrites [48,49].”
Metabolism and Interplay of Reactive Oxygen and Nitrogen Species in Plant Mitochondria
Igamberdiev, A. U., & Bykova, N. V. (2019) · Springer eBooks · doi:10.1007/978-3-030-11129-8_5 · Cited by 6
Dietary Nitrite: from menace to marvel
Bryan, N. S. (2016) · Functional Foods in Health and Disease · doi:10.31989/ffhd.v6i11.295 · Cited by 6
“linked to the mitochondrial electron transport system [47, 48], protonation [45], deoxyhemoglobin [43], and xanthine oxidase [49, 50].”
BackgroundAn Overview of Nitrite and Nitrate
Bryan, N. S. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-805413-0.00003-x · Cited by 6
The existence and significance of redox-cycling ubiquinone in lysosomes
Nohl, H., & Gille, L. (2001) · PROTOPLASMA · doi:10.1007/bf01289407 · Cited by 6
Self-citationRôle pro- et anti-apoptotique du monoxyde d’azote, NO
Kolb, J. (2001) · Comptes Rendus de l Académie des Sciences - Series III - Sciences de la Vie · doi:10.1016/s0764-4469(01)01315-4 · Cited by 6
Nitrate, nitrite and nitric oxide in gastric mucosal defense.
Petersson, J. H. (2008) · Uppsala University Publications (Uppsala University) · Cited by 6
Buerk, D. G., Liu, Y., Zaccheo, K. A., Barbee, K. A., & Jaron, D. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.01053 · Cited by 6
“There is evidence that cytochrome c in the mitochondria can be a source of NO by reducing nitrite (Kozlov et al., 1999).”
BackgroundCortés‐Puch, I., Sun, J., Schechter, A. N., Solomon, S. B., Park, J. W., Feng, J., Gilliard, C. N., Natanson, C., & Piknova, B. (2019) · Nitric Oxide · doi:10.1016/j.niox.2019.07.001 · Cited by 5
“Two major pathways contribute to NO generation in mammals [14]; the well-established Larginine-NO synthase-NO (NOS) pathway [15], and the recently discovered nitrate-nitriteNO reduction pathway [14,16].”
BackgroundAnaerobic Growth and Maintenance of Mammalian Cell Lines
Plotkin, B. J., Sigar, I. M., Swartzendruber, J. A., & Kaminski, A. (2018) · Journal of Visualized Experiments · doi:10.3791/58049 · Cited by 6
Nitric Oxide Synthesis in the Mitochondria of Animal Cells
Rőszer, T. (2012) · Springer eBooks · doi:10.1007/978-94-007-2819-6_10 · Cited by 4
Fat-Soluble Vitamins and Nonnutrients
Kohlmeier, M. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-387784-0.00009-2 · Cited by 3
Nunes, C., & Laranjinha, J. A. N. (2023) · BioChem · doi:10.3390/biochem3020006 · Cited by 4
Ov, A., Korkach, Y. P., & Sagach, V. F. (2024) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-024-03154-z · Cited by 5
“…2018), mARC proteins present in the mitochondrial outer membrane (Klein et al. 2012), microbiota present in mammals’ organism (Ahmed et al. 2017; Liu et al. 2023; Bender and Schwarz 2018), and the ability of mitochondria to reduce nitrate and nitrite (Kozlov et al. 1999; Bombicino et al. 2016).”
Nitrite as endothelial NO donor under anoxia
van Faassen, E. E., Vanin, A. F., & Slama‐Schwok, A. (2007) · Elsevier eBooks · doi:10.1016/b978-044452236-8/50014-9 · Cited by 4
Nitric Oxide as an Alternative Electron Carrier During Oxygen Deprivation
Igamberdiev, A. U., Baron, K. N., & Hill, R. D. (2007) · Springer eBooks · doi:10.1007/7089_2006_096 · Cited by 4
“Both mitochondrial complex III and cytochrome c oxidase could serve as putative sites of nitrite reduction to NO.”
BackgroundInfluentialRedox State in Plant Mitochondria and its Role in Stress Tolerance
Bykova, N. V., & Igamberdiev, A. U. (2016) · Springer eBooks · doi:10.1007/978-3-319-44081-1_5 · Cited by 4
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Thioredoxin and glutaredoxin systems under oxidative and nitrosative stress
Ren, X. (2017) · Figshare · Cited by 4
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“In spite of this, the possible cytoprotective role of cytochrome-mediated NO production was also proposed.(24) In the reported article of protein S-nitrosylation during preconditioning and ischemia/reperfusion injury, the S-nitrosylated site of cytochrome c oxidase subunit 5B (COX5B, Cys115) and of the cytochrome b-c1…”
BackgroundRőszer, T. (2012) · Springer eBooks · doi:10.1007/978-94-007-2819-6_1 · Cited by 3
Nitrite to nitric oxide interconversion by heme FeII complex assisted by [CuI(tmpa)]+
Turias, F., Solà, M., Falivene, L., Cavallo, L., & Poater, A. (2015) · Structural Chemistry · doi:10.1007/s11224-015-0670-0 · Cited by 3
Organic nitrates and nitrites as stores of NO bioactivity
Thatcher, G. R. J. (2007) · Elsevier eBooks · doi:10.1016/b978-044452236-8/50017-4 · Cited by 3
Metadata
- Authors
- Kozlov, A. V., Staniek, K., & Nohl, H.
- Affiliations
- University of Veterinary Medicine Vienna (AT)
- Corresponding author
- Nohl, Hans
- ORCID
- Kozlov, Andrey V
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1999-07-02
- Volume
- 454
- Issue
- 1-2
- Pages
- 127-130
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2149980494
- Cited by
- 342
- References
- 14
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 5 · 2023: 4 · 2022: 8 · 2021: 4 · 2020: 9 · 2019: 15 · 2018: 11 · 2017: 16 · 2016: 14 · 2015: 22 · 2014: 15 · 2013: 9 · 2012: 17
- FWCI
- 2.29
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- 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 › Coenzyme Q10 studies and effects
- Keywords
- nitrite reductase, mitochondria, nitric oxide degradation, nitrite, bc1 complex, ubisemiquinone, myxothiazol, redox cycling, superoxide, electron transport chain
- MeSH terms
- Animals, Electron Spin Resonance Spectroscopy, Electron Transport, Liver, Mitochondria, Models, Biological, Nitric Oxide, Nitrite Reductases, Cell Respiration, Rats
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