Nitric Oxide and Mitochondrial Signaling: From Physiology to Pathophysiology
Abstract
Nitric oxide (NO) has been known for many years to bind to cytochrome C oxidase, the terminal acceptor in the mitochondrial electron transport chain, in competition with oxygen. This interaction may be significant in vivo and explain some of the biological actions of NO. In this article we review the evidence showing that binding of NO to cytochrome C oxidase elicits intracellular signaling events, including the diversion of oxygen to nonrespiratory substrates and the generation of reactive oxygen species. We discuss findings indicating that these NO-elicited events act as triggers by which mitochondria modulate signal transduction cascades involved in the induction of cellular defense mechanisms and adaptive responses. We also discuss instances in which the effects of NO on the electron transport chain might lead to mitochondrial dysfunction and pathology.
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The mitochondrion is a physiological target for NO.
“In the last 15 years it has been established that the mitochondrion is a physiological target for NO (ref. 8).”
From Nitrate and nitrite in biology, nutrition and therapeutics (2009) · cites this paper as [8]
In a double-blind, placebo-controlled, crossover study, Larsen et al. found that oxygen cost during standardized exercise was reduced after 3 days of dietary supplementation with sodium nitrate compared with placebo.
“In a doubleblind, placebo-controlled, cross over study, Larsen et al. found that the oxygen cost during standardized exercise was reduced after 3 days of dietary supplementation with sodium nitrate compared with placebo.124”
From Nitrate-Nitrite-Nitric Oxide Pathway: Implications for Anesthesiology and Intensive Care (2010) · cites this paper as [124]
The Nitric Oxide section discusses how nitric oxide affects cellular respiration and oxygen consumption, but does not report the described exercise study. Searches for Larsen, sodium nitrate, and three-day dietary supplementation found no passage addressing the claimed placebo-controlled result. (LLM, conf=0.74)
Experimental — accuracy not yet measuredIn that study, there was no difference in lactate formation, indicating no compensatory increase in glycolytic energy contribution, and metabolic efficiency seemed to be improved.
“There was no difference in lactate formation, indicating that there was no compensatory increase in glycolytic energy contribution, and thus metabolic efficiency seemed to be improved.”
From Nitrate-Nitrite-Nitric Oxide Pathway: Implications for Anesthesiology and Intensive Care (2010) · cites this paper as [124]
The 'Modulation of Glycolytic Output' section discusses increased glycolysis in certain cells, but does not report lactate formation in the study described by the claim. Searches for lactate and metabolic efficiency found no passage establishing unchanged lactate formation, no compensatory glycolytic increase, or improved metabolic efficiency. No page number is available in our copy. (LLM, conf=0.76)
Experimental — accuracy not yet measuredRecent data suggest that many biologic effects of nitrite involve interaction with mitochondria.
“Recent data suggest that many of the biologic effects of nitrite involve interaction with mitochondria.124,125”
From Nitrate-Nitrite-Nitric Oxide Pathway: Implications for Anesthesiology and Intensive Care (2010) · cites this paper as [124]
The Nitric Oxide section and the supplied Abstract passage describe nitric oxide (NO) interacting with mitochondria, not nitrite. Searches for nitrite and nitrite reduction found no passage in our copy addressing whether nitrite’s biological effects involve mitochondria; page numbers were not available. (LLM, conf=0.78)
Experimental — accuracy not yet measuredThe high affinity and rapid binding of NO to ferrous heme are important biologically for regulation of mitochondrial respiration at CcOx.
“The high affinity and rapid binding to ferrous heme are important biologically for the activation of sGC to generate the second messenger cGMP and the regulation of mitochondrial respiration at CcOx (9–16).”
From What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology (2010) · cites this paper as [12]
The high affinity and rapid binding of NO to ferrous heme are important biologically for activation of sGC to generate cGMP.
“The high affinity and rapid binding to ferrous heme are important biologically for the activation of sGC to generate the second messenger cGMP and the regulation of mitochondrial respiration at CcOx (9–16).”
From What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology (2010) · cites this paper as [12]
NO stabilization of HIF-1α increases glycolytic pathways and activates AMPK.
“Other studies indicate that stabilization of HIF-1α by NO leads to an increase in glycolytic pathways [217] as well as activation of AMPK [218].”
From Signaling and stress: The redox landscape in NOS2 biology (2015) · cites this paper as [218]
A principal regulator of the response to hypoxia is the hypoxia-inducible factor (HIF) family of transcription factors.
“A principal regulator of the response to hypoxia is the hypoxia-inducible factor (HIF) family of transcription factors (31, 61, 115, 165, 177, 185, 221, 282–286, 316, 327).”
From Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function (2009) · cites this paper as [115]
Superoxide reacts rapidly with nitric oxide, generating peroxynitrite, which can impair proteins involved in electron transport.
“Moreover, superoxide is known to react very rapidly with NO (107), generating a damaging peroxynitrite (ONOO−) radical (98, 144, 246), which can impair proteins involved in electron transport (261).”
From Mitochondrial Dysfunction in Diabetes: From Molecular Mechanisms to Functional Significance and Therapeutic Opportunities (2010) · cites this paper as [98]
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- Authors
- Erusalimsky, J. D., & Moncada, S.
- Affiliations
- University College London (GB)
- Venue
- Arteriosclerosis, Thrombosis, and Vascular Biology
- Published
- 2007-12
- Volume
- 27
- Issue
- 12
- Pages
- 2524-2531
- ISSN
- 1079-5642 (ISSN-L)
- 1524-4636
- OpenAlex
- W2048626265
- Cited by
- 336
- References
- 105
- Citations by year
- 2026: 2 · 2025: 8 · 2024: 15 · 2023: 6 · 2022: 11 · 2021: 15 · 2020: 9 · 2019: 10 · 2018: 6 · 2017: 16 · 2016: 13 · 2015: 19 · 2014: 34 · 2013: 30 · 2012: 21
- FWCI
- 3.23
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Arteriosclerosis Thrombosis and Vascular Biology (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Research Explorer (The University of Manchester) (submittedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- nitric oxide, cytochrome c oxidase, mitochondrial signaling, electron transport chain, reactive oxygen species, signal transduction, cellular defense mechanisms, mitochondrial dysfunction
- MeSH terms
- Animals, Calcium, Electron Transport Complex IV, Endothelium, Vascular, Glycolysis, Homeostasis, Humans, Mitochondria, Multienzyme Complexes, Nitric Oxide, Oxygen, Transcription Factors, Signal Transduction, Cell Hypoxia, Apoptosis, Protein Serine-Threonine Kinases, Reactive Oxygen Species, Cytoprotection, Endothelial Cells, Membrane Potential, Mitochondrial, AMP-Activated Protein Kinases
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