| TCID | Name | Domain | Kingdom/Phylum | Protein(s) |
|---|---|---|---|---|
|
3.D.10.1.1 | Succinate:menaquinone oxidoreductase, SdhABC (pmf consuming when starting with succinate; pmf generating when starting with fumarate (the reverse reaction)). Transmembrane electron transfer is coupled to protolytic reactions on opposite sides of the membrane, allowing the transmembrane pmf to drive the endergonic oxidation of succinate by menaquinone by the dihaem-containing SQR (Lancaster et al. 2008). | Bacteria |
Bacillota | SdhABC of Bacillus licheniformis SdhA (flavoprotein; 587aas) (Q65GF4) SdhB (iron-sulfur center subunit; 254aas) (Q65GF5) SdhC (transmembrane cytochrome c558 subunit; 202aas) (Q65GF3) |
|
3.D.10.1.2 | Succinate dehydrogenase/fumarate reductase, SdhABC. | Bacteria |
Spirochaetota | Succinate dehydrogenase/fumarate reductase, SdhABC, of Leptospira interrogans |
|
3.D.10.1.3 | The diheme-containing quinol:fumarate reductase (QFR), FrdABC (Madej et al. 2009). This enzyme complex is required for fumarate respiration using formate or sulfide as electron donor. It mediates transmembrane electron transfer by proton transfer via a compensatory transmembrane proton transfer pathway ('E-pathway') (Lancaster et al. 2008). This is necessary because, although the reduction of fumarate by menaquinol is exergonic, it is not exergonic enough to support the generation of a pmf. This compensatory E-pathway appears to be required by all dihaem- containing QFR enzymes. The conservation of an essential acidic residue on transmembrane helix V (Glu-C180 in W. succinogenes QFR) provides a key for the sequence-based discrimination of these QFR enzymes from the dihaem-containing SQR enzymes (Lancaster et al. 2008). This enzyme complex may mediate transmembrane electron transfer coupled to protolytic reactions on opposite sides of the membrane and by transmembrane proton transport (Madej et al. 2006). | Bacteria |
Campylobacterota | FrdABC of Wolinella succinogenes (Vibrio succinogenes) |
|
3.D.10.1.4 | Succinate dehydrogenase, SdhABC, or type E succinate:quinone oxidoreductase (SQR) (Hamann et al. 2009). | Archaea |
Thermoproteota | SDH of Sulfolobus tokodaii (S. sulfataricus) |
|
3.D.10.1.5 | Three subunit menaquinone:fumarate oxidoreductase (QfrABC or SdhABC ) (Xin et al. 2009). | Bacteria |
Chlorobiota | QfrABC of Chlorobium tepidum QfrA, 646 aas (flavoprotein; FAD-containing) QfrB, 257 aas (iron-sulfur protein) QfrC, 240 aas and 5 TMSs (contains two b-type hemes and two menaquinones) |
|
3.D.10.1.6 | Succinate dehydrogenase complex, SdhABCD. SdhA, 598 aas and 1 TMS. Flavoprotein subunit, X5H3P0. | Bacteria |
Pseudomonadota | SdhABCD of Neorickettsia helminthoeca |
|
3.D.10.1.7 | Succinate dehydrogenase complex, or succinate:ubiquinone oxidoreductase (SQR) or mitochondrial respiratory complex II of four subunits, SdhA, B, C and D. Does not transport protons across the membrane, but all 4 subunits are homologous to the prokaryotic Sdh subunits that do transport protons. It is an integral membrane protein complex in both the tricarboxylic acid cycle and aerobic respiration. Sun et al. 2005 reported the first crystal structure of Complex II from porcine heart at 2.4 Å resolution and its complex structure with inhibitors 3-nitropropionate and 2-thenoyltrifluoroacetone (TTFA) at 3.5 Å resolution. Complex II is comprised of two hydrophilic proteins, flavoprotein (Fp) and iron-sulfur protein (Ip), and two transmembrane proteins (CybL and CybS), as well as prosthetic groups required for electron transfer from succinate to ubiquinone. The structure correlates the protein environments around prosthetic groups with their unique midpoint redox potentials. Two ubiquinone binding sites are identified. The structure provides a bona fide model for study of the mitochondrial respiratory system and human mitochondrial diseases related to mutations in this complex (Sun et al. 2005). the loss of electron transfer Complex II (succcinate dehydrogenase), but not that of Complex I, reduces melanoma tumor growth by increasing antigen presentation and T cell-mediated killing. This is driven by succinate-mediated transcriptional and epigenetic activation of major histocompatibility complex-antigen processing and presentation (MHC-APP) genes independent of interferon signaling (Mangalhara et al. 2023). | Eukaryota |
Metazoa, Chordata | Sdh complex of Homo sapiens |
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3.D.10.1.8 | Quinol:fumarate reductase respiratory complex, FrdABC, where FrdA (627 aas) and FrdB (264 aas) are soluble proteins while FrdC has 218 aas and 5 TMSs. The crystal structure has been determined at 3.6 Å resolution (Guan et al. 2018). QFR in anaerobic bacteria catalyzes the reduction of fumarate to succinate by quinol in the anaerobic respiratory chain. The electron/proton-transfer pathway in the anaerobic sulphate-reducing bacterium Desulfovibrio gigas involves a homo-dimer, each protomer comprising two hydrophilic subunits, A and B, and one transmembrane subunit C, together with six redox cofactors including two b-hemes. One menaquinone molecule is bound near heme bL in the hydrophobic subunit C. This location of the menaquinone-binding site differs from the menaquinol-binding cavity proposed previously for QFR from Wolinella succinogenes (TC#3.D.10.1.3). The bound menaquinone may serve as an additional redox cofactor to mediate the proton-coupled electron transport across the membrane. Guan et al. 2018 proposed electron/proton-transfer pathways during the quinol-dependent reduction of fumarate to succinate in the D. gigas QFR. | Bacteria |
Thermodesulfobacteriota | QfrABC of Desulfovibrio gigas |
|
3.D.10.1.9 | Succinate dehydrogenase with 5 subunits, Sdh2, SdhABCDF. The cryo-EM structure of trimeric Mycobacterium smegmatis succinate dehydrogenase with a membrane-anchor, SdhF, has been determined (Gong et al. 2020). Diheme-containing succinate:menaquinone oxidoreductases (Sdh) are widespread in Gram-positive bacteria. Gong et al. 2020 presented the 2.8 Å cryo-EM structure of Sdh, which forms a trimer with a membrane-anchored SdhF as a subunit of the complex (PDB 6LUM). The 3 kDa SdhF forms a single transmembrane helix, and this helix plays a role in blocking the canonically proximal quinone-binding site. The authors also identified two distal quinone-binding sites with bound quinones. One distal binding site is formed by neighboring subunits of the complex, and the electron/proton transfer pathway for succinate oxidation by menaquinone was revealed. The structure provides insight into the physiological significance of a trimeric respiratory complex II. The structure of the menaquinone binding site could provide a framework for the development of Sdh-selective anti-mycobacterial drugs (Gong et al. 2020). The architecture of SdhABC (type F), with a membrane-embedded Rieske FeS cluster, has been solved to 2.5 Å resolution (Zhou et al. 2021). A quinone-binding site and a rarely observed Rieske-type [2Fe-2S] cluster, the latter being embedded in the transmembrane region, were identified, and an electron transfer pathway that connects the substrate-binding and quinone-binding sites was identified (Zhou et al. 2021). | Bacteria |
Actinomycetota | SdhABCDF of Mycolicibacterium smegmatis (strain ATCC 700084) (Mycobacterium smegmatis) SdhA, 584 aas, I7FYK4, flavoprotein subunit SdhB, 261 aas, I7G4J1, iron-sulfur protein SdhC, 144 aas and 3 TMSs, I7G657, cytochrome B-556 subunit SdhD, 156 aas and 3 TMSs, I7FGY0, hydrophobic membrane anchor protein SdhF, subunit of SDH, of 32 aas and one TMS, AWT56629.1 |