Mechanism of superoxide and hydrogen peroxide formation by fumarate reductase, succinate dehydrogenase, and aspartate oxidase
Open accessAbstract
Oxidative stress is created in aerobic organisms when molecular oxygen chemically oxidizes redox enzymes, forming superoxide (O2*-) and hydrogen peroxide (H2O2). Prior work identified several flavoenzymes from Escherichia coli that tend to autoxidize. Of these, fumarate reductase (Frd) is notable both for its high turnover number and for its production of substantial O2*- in addition to H2O2. We have sought to identify characteristics of Frd that predispose it to this behavior. The ability of excess succinate to block autoxidation and the inhibitory effect of lowering the flavin potential indicate that all detectable autoxidation occurs from its FAD site, rather than from iron-sulfur clusters or bound quinones. The flavin adenine dinucleotide (FAD) moiety of Frd is unusually solvent-exposed, as evidenced by its ability to bind sulfite, and this may make it more likely to react adventitiously with O2*-. The autoxidizing species is apparently fully reduced flavin rather than flavosemiquinone, since treatments that more fully reduce the enzyme do not slow its turnover number. They do, however, switch the major product from O2*- to H2O2. A similar effect is achieved by lowering the potential of the proximal [2Fe-2S] cluster. These data suggest that Frd releases O2*- into bulk solution if this cluster is available to sequester the semiquinone electron; otherwise, that electron is rapidly transferred to the nascent superoxide, and H2O2 is the product that leaves the active site. This model is supported by the behavior of "aspartate oxidase" (aspartate:fumarate oxidoreductase), an Frd homologue that lacks Fe-S clusters. Its dihydroflavin also reacts avidly with oxygen, and H2O2 is the predominant product. In contrast, succinate dehydrogenase, with high potential clusters, generates O2*- exclusively. The identities of enzyme autoxidation products are significant because O2*- and H2O2 damage cells in different ways.
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E. coli SQR and QFR both produce ROS with a linear dependence on dissolved oxygen, although SQR produces ROS at a much lower rate.
“Both enzymes produced ROS with a linear dependence on the dissolved oxygen concentration, although SQR produced ROS at a much lower rate.”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [101]
E. coli SQR exclusively produces superoxide, whereas QFR produces mainly superoxide at lower succinate concentrations and relatively more hydrogen peroxide at higher succinate concentrations.
“E. coli SQR exclusively produces superoxide.In contrast, E. coli QFR produces mainly superoxide at lower succinate concentrations and comparably more hydrogen peroxide at higher substrate concentrations [101].”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [101]
The most likely ROS source in wild-type complex II is the fully reduced FAD, although a Q-site contribution might occur in mutants.
“While a contribution of the Q site might occur in the respective mutants, the most likely source of ROS in wild-type complex II is the fully reduced FAD [37,101].”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [101]
Messner and Imlay concluded that QFR releases superoxide from fully reduced flavin if the [2Fe-2S] cluster is available to sequester the semiquinone electron; otherwise the electron is rapidly transferred to nascent superoxide and hydrogen peroxide is released.
“Messner and Imlay concluded that QFR releases superoxide from the fully reduced flavin if the [2Fe-2S] cluster is available to sequester the semiquinone electron; otherwise this electron is rapidly transferred to the nascent superoxide and hydrogen peroxide is released [101].”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [101]
Fully reduced FAD can transfer one electron to molecular oxygen to form superoxide, probably the major reaction in complex II but only confirmed for E. coli SQR, or transfer both electrons to O2 to form hydrogen peroxide, as shown for E. coli QFR.
“In principle, fully reduced FAD can either transfer one electron onto molecular oxygen which leads to the formation of superoxide (probably the major reaction in complex II, but only confirmed for E. coli SQR [101]) or it may also transfer both electrons onto O 2 which leads to the formation of H 2 O 2 (as shown for E. coli QFR [101]) (Fig. 2B).”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [101]
Impairment in the normal removal of electrons from the flavin group in SdhA could promote superoxide generation through autoxidation of the reduced flavin group by O2 in the matrix.
“An impairment in the normal removal of electrons from the flavin group in SdhA could promote superoxide generation through the autoxidation of the reduced flavin group by O 2 in the matrix (34, 38, 46, 51).”
From Loss of the SdhB, but Not the SdhA, Subunit of Complex II Triggers Reactive Oxygen Species-Dependent Hypoxia-Inducible Factor Activation and Tumorigenesis (2008) · cites this paper as [34]
Some evidence suggests that the flavin adenine dinucleotide site in SdhA is the principal source of superoxide generation.
“Some evidence suggests that the flavin adenine dinucleotide site in SdhA is the principal source of superoxide generation, due to the exposure of that moiety to the aqueous environment and the high electron density that develops when the electron flux downstream from that site is obstructed (34, 51).”
From Loss of the SdhB, but Not the SdhA, Subunit of Complex II Triggers Reactive Oxygen Species-Dependent Hypoxia-Inducible Factor Activation and Tumorigenesis (2008) · cites this paper as [34]
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“The first suggested that reactive oxygen species (ROS) from an impaired complex II of the electron transport chain (18, 30) potentially inhibit PHDs (7).”
BackgroundHow oxygen attacks [FeFe] hydrogenases from photosynthetic organisms
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Cadmium-Induced Oxidative Stress: Focus on the Central Nervous System
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“Several reports have indicated that bacterial dehydrogenases are important enzymes in oxidative stress response, such as NADH dehydrogenase, lactate dehydrogenase, formate dehydrogenase, succinate dehydrogenase, fumarate reductase, and glutathione-dependent formaldehyde dehydrogenase [27-32].”
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“Rather, the primary impact of 4HNE is to covalently bind SDHA disrupting the functionality of this molecule so that it auto-oxidizes and adventitiously transfers electrons to oxygen in the manner described by Messner and Imlay (35).”
BackgroundBiochemical dysfunction in heart mitochondria exposed to ischaemia and reperfusion
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“This would not only cause succinate to accumulate but additionally will cause ROS generation because fumarate reductase has been demonstrated to be a powerful O2•− generator (e.g., Imlay, 1995; Messner and Imlay, 2002; Turrens, 1987).”
Mitochondrial Complex II in the Post-ischemic Heart
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How radiation kills cells: Survival of and under oxidative stress
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BackgroundInfluentialAre Respiratory Enzymes the Primary Sources of Intracellular Hydrogen Peroxide?
Seaver, L. C., & Imlay, J. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408754200 · Cited by 223 · see citing works
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The disulfide relay system of mitochondria is connected to the respiratory chain
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“The mitochondrial IMS is anyway highly at risk of the ROS production by respiratory chain complexes (Guo and Lemire, 2003; Kussmaul and Hirst, 2006; Messner and Imlay, 2002; Sun and Trumpower, 2003; Yankovskaya et al., 2003).”
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The respiratory chain of Corynebacterium glutamicum
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“Although our in vitro data and the studies cited above indicate Complex III as the main site of ROS release, other studies of Complex II in mitochondria from yeast and various tissues suggest that this complex is also a potential site of ROS production [16,47–49].”
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“) to ubiquinol (QH2) by means of the electrons (e–) derived from the oxidation of succinate to fumarate in the Krebs cycle, and/or the complete transfer of the electrons through MTCII prevents their accumulation in the flavoprotein and iron-sulfur subunits, which might lead to ROS production through chemical interacti…”
BackgroundThe assembly of succinate dehydrogenase: a key enzyme in bioenergetics
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Two sources of endogenous hydrogen peroxide in Escherichia coli
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“…to the form that we now know as succinate dehydrogenase: the elevation of its iron-sulphur cluster potentials and the addition of an accessory haem pull electron density away from the flavin and thereby strongly suppresses its oxidation rate (Messner and Imlay, 2002; Yandovskaya et al., 2003).”
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“22 V) is the direct electron donor (31).”
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“Mitochondria are a major source of reactive oxygen species (ROS), from sites within the ETC (117, 128, 167, 230) and the Krebs cycle (231).”
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“In addition, ROS can be produced by the impairment of SDH/complex II (Figure 5) [91], and 3-BrPA could inhibit this respiratory enzyme.”
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Genome‐scale model for Clostridium acetobutylicum: Part I. Metabolic network resolution and analysis
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Real-time electron transfer in respiratory complex I
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“Therefore, our finding is consistent with the proposal that an Fe/S center near the flavin captures the electron from the FMN radical before it can react with nascent superoxide to form hydrogen peroxide (17).”
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“Many scientists in the field of cancer research may have considered mitochondria only as a reservoir for stocking harmful molecules such as ROS and apoptotic proteins.”
BackgroundInfluentialMitochondrial complex II and reactive oxygen species in disease and therapy
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“in normal cells) [36,47,55], this is not the case for S.”
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How Microbes Defend Themselves From Incoming Hydrogen Peroxide
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“The small size of O2 prevents its exclusion from most active sites, and its collision with reduced flavins triggers the consecutive transfer of one or two electrons, generating O2 or H2O2, respectively (19).”
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“5), causing electrons to “pile up” in the respiratory electron transport chain (26).”
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“The major source of endogenous ROS in E. coli is a result of auto-oxidation of components of the aerobic respiratory chain (i.e., NADH dehydrogenase [complex I] and succinate dehydrogenase [complex II], as well as fumarate reductase) (124, 167, 168, 178), leading to the generation of 5 (cid”
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“Aside from the NADH-driven ROS production from complex I and subsequently complex III, complex II has also been demonstrated as a source of ROS production (Gleason et al., 2011; Messner and Imlay, 2002; Quinlan et al., 2012; Zhang et al., 1998).”
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“Similar mechanisms have been proposed previously, for xanthine oxidase, fumarate reductase, and succinate dehydrogenase (47, 48).”
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Protein-mediated assembly of succinate dehydrogenase and its cofactors
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“This oxidation causes a reduction of the FAD cofactor, which then reduces molecular oxygen to form superoxide (Messner & Imlay, 2002).”
BackgroundHow Microbes Evolved to Tolerate Oxygen
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SDHAF4 Promotes Mitochondrial Succinate Dehydrogenase Activity and Prevents Neurodegeneration
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“We propose that this unique demand might relate to the need to protect the redoxactive cofactors present in many ETC complex subunits (Messner and Imlay, 2002).”
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“The metabolic pathways ArcA controls are large sources of internal ROS production and thus may need to be repressed when the cell faces an exogenous ROS threat (206, 207).”
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“The aerobic respiratory chain is not only a main source of ATP but it also a major source of reactive oxygen species (ROS; Gonzalez-Flecha and Demple, 1995; Messner and Imlay, 2002; Mailloux et al., 2011).”
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“The enzyme isolated from Escherichia coli or purified from bovine heart has been reported to generate superoxide under some conditions (Messner & Imlay, 2002; Zhang, Yu, & Yu, 1998).”
Mitochondrial production of reactive oxygen species
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“Strikingly, obligate anaerobes may have high titres of low-potential flavoproteins, such as fumarate reductase, that are easily oxidized by molecular oxygen (Imlay, 1995; Messner and Imlay, 2002).”
BackgroundSelf-citationHow Escherichia coli Tolerates Profuse Hydrogen Peroxide Formation by a Catabolic Pathway
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“Respiratory molecules are a source of intracellular ROS (Messner and Imlay, 1999; 2002; Seaver and Imlay, 2004).”
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Superoxide Destroys the [2Fe-2S]2+ Cluster of FNR from Escherichia coli
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- Authors
- Messner, K. R., & Imlay, J. A.
- Affiliations
- University of Illinois Urbana-Champaign (US)
- Corresponding author
- Imlay, James A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-11
- Volume
- 277
- Issue
- 45
- Pages
- 42563-42571
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2044412059
- Cited by
- 301
- References
- 57
- Citations by year
- 2026: 9 · 2025: 4 · 2024: 12 · 2023: 11 · 2022: 15 · 2021: 14 · 2020: 18 · 2019: 13 · 2018: 17 · 2017: 14 · 2016: 8 · 2015: 12 · 2014: 16 · 2013: 21 · 2012: 18
- FWCI
- 3.36
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (GM49640)
- National Institute of General Medical Sciences (R01GM049640, GM 49640, T32 GM07283-20, T32GM007283)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Keywords
- fumarate reductase, succinate dehydrogenase, superoxide production, hydrogen peroxide production, FAD, flavin semiquinone, [2Fe-2S] cluster, oxidative stress, Escherichia coli
- MeSH terms
- Amino Acid Oxidoreductases, Cell Line, Cell Membrane, Escherichia coli, Flavin-Adenine Dinucleotide, Hydrogen Peroxide, Iron-Sulfur Proteins, Kinetics, Oxidation-Reduction, Solvents, Succinate Dehydrogenase, Superoxides, D-Aspartate Oxidase
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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