Conformational Change of Mitochondrial Complex I Increases ROS Sensitivity During Ischemia
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AIMS: Myocardial ischemia/reperfusion (I/R) is associated with mitochondrial dysfunction and subsequent cardiomyocyte death. The generation of excessive quantities of reactive oxygen species (ROS) and resultant damage to mitochondrial enzymes is considered an important mechanism underlying reperfusion injury. Mitochondrial complex I can exist in two interconvertible states: active (A) and deactive or dormant (D). We have studied the active/deactive (A/D) equilibrium in several tissues under ischemic conditions in vivo and investigated the sensitivity of both forms of the heart enzyme to ROS. RESULTS: We found that in the heart, t½ of complex I deactivation during ischemia was 10 min, and that reperfusion resulted in the return of A/D equilibrium to its initial level. The rate of superoxide generation by complex I was higher in ischemic samples where content of the D-form was higher. Only the D-form was susceptible to inhibition by H2O2 or superoxide, whereas turnover-dependent activation of the enzyme resulted in formation of the A-form, which was much less sensitive to ROS. The mitochondrial-encoded subunit ND3, most likely responsible for the sensitivity of the D-form to ROS, was identified by redox difference gel electrophoresis. INNOVATION: A combined in vivo and biochemical approach suggests that sensitivity of the mitochondrial system to ROS during myocardial I/R can be significantly affected by the conformational state of complex I, which may therefore represent a new therapeutic target in this setting. CONCLUSION: The presented data suggest that transition of complex I into the D-form in the absence of oxygen may represent a key event in promoting cardiac injury during I/R.
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Cys39 of ND3 has been shown to become exposed under hypoxia or lack of NADH that result in low complex I activity due to the active-deactive transition.
“Notably, one of these, Cys39 of the ND3 subunit, has been shown to become exposed under conditions of hypoxia or lack of NADH that result in low complex I activity due to the active-deactive transition26–28.”
From Cardioprotection by S-nitrosation of a cysteine switch on mitochondrial complex I (2013) · cites this paper as [28]
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- Authors
- Gorenkova, N., Robinson, E., Grieve, D. J., & Galkin, A.
- Affiliations
- Queen's University Belfast (GB)
- Royal Victoria Hospital (GB)
- Corresponding author
- Galkin, Alexander
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2013-11
- Volume
- 19
- Issue
- 13
- Pages
- 1459-1468
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- PMC
- PMC3797456
- OpenAlex
- W2075349874
- Cited by
- 82
- References
- 55
- Citations by year
- 2026: 1 · 2025: 6 · 2024: 4 · 2023: 3 · 2022: 4 · 2021: 7 · 2020: 4 · 2019: 16 · 2018: 12 · 2017: 4 · 2016: 8 · 2015: 4 · 2014: 5 · 2013: 4
- FWCI
- 5.24
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Antioxidants and Redox Signaling (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Research Portal (Queen's University Belfast) (acceptedVersion, other-oa)
- Funders
- British Heart Foundation (PG/09/102/28133)
- University of St Andrews
- Medical Research Council (G1100051)
- Topics
- Health Sciences › Medicine › Pathology and Forensic Medicine › Cardiac Ischemia and Reperfusion
- 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
- mitochondrial complex I, conformational change, reactive oxygen species, myocardial ischemia-reperfusion injury, superoxide production, hydrogen peroxide sensitivity, redox sensitivity, cardiomyocyte death, mitochondrial dysfunction
- MeSH terms
- Animals, Female, Mice, Inbred C57BL, Protein Conformation, Myocardial Ischemia, Reactive Oxygen Species, Electron Transport Complex I, Mice
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