Superoxide generation by complex III: From mechanistic rationales to functional consequences

Bleier, Lea; Dröse, Stefan

doi:10.1016/j.bbabio.2012.12.002

Cited by 369Mitochondrial Function and PathologyCoenzyme Q10 studies and effectsRedox biology and oxidative stress

Superoxide generation by complex III: From mechanistic rationales to functional consequences

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Bleier, Lea, Dröse, Stefan·2013·Biochimica et Biophysica Acta (BBA) - Bioenergetics

DOI 10.1016/j.bbabio.2012.12.002

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Abstract

Apart from complex I (NADH:ubiquinone oxidoreductase) the mitochondrial cytochrome bc1 complex (complex III; ubiquinol:cytochrome c oxidoreductase) has been identified as the main producer of superoxide and derived reactive oxygen species (ROS) within the mitochondrial respiratory chain. Mitochondrial ROS are generally linked to oxidative stress, aging and other pathophysiological settings like in neurodegenerative diseases. However, ROS produced at the ubiquinol oxidation center (center P, Qo site) of complex III seem to have additional physiological functions as signaling molecules during cellular processes like the adaptation to hypoxia. The molecular mechanism of superoxide production that is mechanistically linked to the electron bifurcation during ubiquinol oxidation is still a matter of debate. Some insight comes from extensive kinetic studies with mutated complexes from yeast and bacterial cytochrome bc1 complexes. This review is intended to bridge the gap between those mechanistic studies and investigations on complex III ROS in cellular signal transduction and highlights factors that impact superoxide generation. This article is part of a Special Issue entitled: Respiratory complex III and related bc complexes.

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The ROS-promoting effect of complex II inhibitors can be explained by a partially oxidized Q-pool that maximizes complex III ROS production during antimycin inhibition.
“This ROS-promoting effect of complex II inhibitors can be related to a partially oxidized Q-pool that maximizes ROS production by complex III upon antimycin inhibition [25,32,33].”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [25]
Inhibiting complex II can raise superoxide generation at the Qo site of complex III when succinate is the main substrate and electron transfer between heme bL and heme bH is slowed, such as when the Qi site is blocked by antimycin A.
“On the other hand, inhibition of complex II can increase the generation of superoxide at the ubiquinol oxidation site (Q o site) of complex III under specific conditions [25], i.e. when succinate is the predominant substrate and when the electron transfer between heme b L (low potential heme) and heme b H (high potential heme) is slowed down additionally, e.g. when the ubiquinone reduction site of”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [25]
Increased oxidation of the Q-pool explains the increased ROS generation by antimycin A-inhibited complex III, because superoxide generation at the Qo site is maximal at intermediate reduction states of the ubiquinone pool when the Qi site is blocked.
“This can be explained by an increased oxidation of the Q-pool, since it was shown that the superoxide generation at the Q o site is maximal at intermediate reduction states of the ubiquinone pool if the Q i site is blocked by antimycin A [25,32,33].”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [25]
Complex II is recognized as a modulator of superoxide production by other mitochondrial enzymes, especially complexes I and III.
“Apart from the direct generation of ROS (Section 3.1), complex II has been recognized as a modulator of the superoxide production by other mitochondrial enzymes, especially the respiratory chain complexes I and III [15,16,25] that are generally regarded as main ROS sources in the mitochondria [3][4][5][6].”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [25]
A physiological correlate of experimentally induced antimycin A inhibition has not been identified.
“However, it has to be pointed out that a physiological correlate of the experimentally induced antimycin A inhibition has not been identified yet [25].”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [25]

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A Minimal Model of Ubiquinol:Cytochrome C Reductase Capable of Simulating Superoxide Production
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Authors: Bleier, L., & Dröse, S.
Affiliations: Goethe University Frankfurt (DE)
Corresponding author: Dröse, Stefan
ORCID: Dröse, Stefan
Venue: Biochimica et Biophysica Acta (BBA) - Bioenergetics
Publisher: Elsevier BV
Published: 2013-11
Volume: 1827
Issue: 11-12
Pages: 1320-1331
ISSN: 0005-2728 (ISSN-L)
DOI: 10.1016/j.bbabio.2012.12.002
OpenAlex: W2222326255
Cited by: 369
References: 186
Citations by year: 2026: 15 · 2025: 31 · 2024: 22 · 2023: 26 · 2022: 31 · 2021: 47 · 2020: 49 · 2019: 31 · 2018: 25 · 2017: 24 · 2016: 25 · 2015: 23 · 2014: 14 · 2013: 6
FWCI: 1.25
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 365 d)
Locations: Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
PubMed (publishedVersion)
Funders: Deutsche Forschungsgemeinschaft (SFB815)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Coenzyme Q10 studies and effects
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords: cytochrome bc1 complex, superoxide production, reactive oxygen species, mitochondrial respiratory chain, electron bifurcation, ubiquinol oxidation, Qo site, hypoxia adaptation, oxidative stress, ROS signaling
MeSH terms: Electron Transport, Heme, Humans, Models, Chemical, Models, Molecular, Protein Conformation, Superoxides, Electron Transport Complex III, Protein Subunits, Mitochondrial Membranes

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Superoxide generation by complex III: From mechanistic rationales to functional consequences

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