Contribution of the FAD and quinone binding sites to the production of reactive oxygen species from Ascaris suum mitochondrial complex II
Abstract
Reactive oxygen species (ROS) production from mitochondrial complex II (succinate-quinone reductase, SQR) has become a focus of research recently since it is implicated in carcinogenesis. To date, the FAD site is proposed as the ROS producing site in complex II, based on studies done on Escherichia coli, whereas the quinone binding site is proposed as the site of ROS production based on studies in Saccharomyces cerevisiae. Using the submitochondrial particles from the adult worms and L(3) larvae of the parasitic nematode Ascaris suum, we found that ROS are produced from more than one site in the mitochondrial complex II. Moreover, the succinate-dependent ROS production from the complex II of the A. suum adult worm was significantly higher than that from the complex II of the L(3) larvae. Considering the conservation of amino acids crucial for the SQR activity and the high levels of ROS production from the mitochondrial complex II of the A. suum adult worm together with the absence of complexes III and IV activities in its respiratory chain, it is a good model to examine the reactive oxygen species production from the mitochondrial complex II.
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In adult Ascaris suum submitochondrial particles, succinate-dependent ROS generation was not affected by a complex I inhibitor and was completely or partially suppressed by malonate or atpenin A5, indicating that complex II was the exclusive ROS source under those conditions.
“The succinate-dependent ROS generation of SMP from adult worms, that do not contain complex III and IV activities in their respiratory chain, was not influenced by a complex I inhibitor and was completely and partially suppressed by malonate or atpenin A5, respectively.This indicates that complex II is the exclusive ROS source under these conditions.”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [100]
E. coli SQR and QFR show maximal ROS at intermediate succinate concentrations between 0.1 and 1 mM and lower rates at lower and higher substrate concentrations, resembling mammalian and nematode complex II.
“Furthermore, both enzymes showed maximal rates of ROS at intermediate succinate concentrations between 0.1 and 1 mM and decreased rates at lower and higher substrate concentration, which resembles the dependence found later for mammalian [37] and nematode [100] complex II.”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [100]
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Mitochondrial redox biology: Reactive species production and antioxidant defenses
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Self-citationAnalysis of Mammalian Succinate Dehydrogenase Kinetics and Reactive Oxygen Species ProductionPreprint
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- Authors
- Paranagama, M. P., Sakamoto, K., Amino, H., Awano, M., Miyoshi, H., & Kita, K.
- Affiliations
- The University of Tokyo (JP)
- Kyoto University (JP)
- Corresponding author
- Sakamoto, Kimitoshi
- Venue
- Mitochondrion
- Publisher
- Elsevier BV
- Published
- 2010-03
- Volume
- 10
- Issue
- 2
- Pages
- 158-165
- ISSN
- 1567-7249 (ISSN-L)
- OpenAlex
- W1995190951
- Cited by
- 40
- References
- 57
- Citations by year
- 2025: 1 · 2023: 1 · 2022: 4 · 2021: 6 · 2020: 1 · 2019: 3 · 2018: 1 · 2016: 2 · 2015: 5 · 2014: 5 · 2013: 4 · 2012: 3
- FWCI
- 0.94
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Mitochondrion (publishedVersion)
- PubMed (publishedVersion)
- Topics
- 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
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Bioactive Compounds and Antitumor Agents
- Keywords
- reactive oxygen species, succinate dehydrogenase, FAD binding site, quinone binding site, Ascaris suum, nematode larvae, adult worms, carcinogenesis, electron transport chain
- MeSH terms
- Animals, Binding Sites, Flavin-Adenine Dinucleotide, Larva, Mitochondria, Benzoquinones, Ascaris suum, Reactive Oxygen Species, Electron Transport Complex II
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