respiratory chain complex II (succinate dehydrogenase)
Respiratory chain complex II (succinate dehydrogenase) is a respiratory-chain enzyme complex that oxidizes succinate, passes electrons through flavin and iron-sulfur centers to membrane quinone, and thereby connects tricarboxylic-acid-cycle electron flow with the respiratory quinone pool. [GO:0045273]
Synonyms: electron transport complex II
Components
| Component | Type | Part of / acts on | Grounding | Genes | Stoichiometry | Essential | Role |
|---|---|---|---|---|---|---|---|
| succinate dehydrogenase flavoprotein subunit | Protein | part of | Reviewed label only (reviewed name; no accession asserted) | sdhA | ESSENTIAL | Catalytic flavoprotein subunit that oxidizes succinate at FAD and begins electron transfer through the complex II soluble head.
| |
| succinate dehydrogenase iron-sulfur subunit | Protein | part of | Reviewed label only (reviewed name; no accession asserted) | sdhB | ESSENTIAL | Iron-sulfur subunit that relays electrons from the FAD site of SdhA toward the membrane quinone-reduction site.
| |
| succinate dehydrogenase SdhCD membrane anchor | Protein complex | part of | Reviewed label only (reviewed name; no accession asserted) | sdhC, sdhD | ESSENTIAL | Membrane-anchor module that binds quinone-site cofactors and connects the soluble succinate-oxidizing subunits to the respiratory membrane.
|
Canonical examples
NCBITaxon:562Escherichia coli — Bacterial source of the four-protein succinate dehydrogenase structure deposited as PDB:1NEK. [PDB:1NEK]
Functions
- succinate dehydrogenase (quinone) activity
GO:0008177— Complex II oxidizes succinate to fumarate while reducing a membrane quinone to quinol.GO:0008177GO:0008177 defines the overall succinate plus quinone to fumarate plus quinol reaction of the entire succinate dehydrogenase complex.DOI:10.1126/science.1079605Yankovskaya et al. 2003 structurally tied the E. coli complex II subunit layout to succinate oxidation and quinone reduction.
Mechanism graphs
Complex II links succinate oxidation to quinone reduction (FUNCTION)
Respiratory complex II accepts electrons from succinate at its flavoprotein, relays them through iron-sulfur centers, and reduces a membrane quinone at its anchor.
| Subject | Predicate | Object | Evidence |
|---|---|---|---|
| succinate | feeds electrons to | succinate dehydrogenase flavoprotein subunit |
|
| succinate dehydrogenase flavoprotein subunit | passes electrons to | succinate dehydrogenase iron-sulfur subunit |
|
| succinate dehydrogenase iron-sulfur subunit | relays electrons toward | succinate dehydrogenase SdhCD membrane anchor |
|
| succinate dehydrogenase SdhCD membrane anchor | binds | ubiquinone Q2 |
|
| respiratory chain complex II (succinate dehydrogenase) | enables | succinate dehydrogenase (quinone) activity |
|
Discussions
- CURATION_TODO (OPEN): Resolve exact source-neutral InterPro, Pfam, NCBIfam, or Complex Portal groundings for respiratory complex II subunits before replacing reviewed-label-only rows. The first record deliberately models the conserved four-polypeptide architecture without asserting that domain-level Pfam matches exactly ground full taxon-agnostic protein families.
Evidence
GO:0045273Gene Ontology cellular-component term for respiratory chain complex II, succinate dehydrogenase.GO:0098803Gene Ontology cellular-component term for respiratory-chain protein complexes.GO:0008177Gene Ontology molecular-function term for the overall succinate dehydrogenase quinone oxidoreductase activity.DOI:10.1126/science.1079605Yankovskaya et al. 2003, Architecture of succinate dehydrogenase and reactive oxygen species generation, Science.PMID:12560550PubMed identifier for Yankovskaya et al. 2003 as reported by the RCSB PDB:1NEK primary citation.PDB:1NEKRCSB Protein Data Bank entry for the E. coli respiratory complex II structure from Yankovskaya et al. 2003.
Curation history
2026-09-24T03:46:49Zcodex · CREATED_RECORD — Scaffolded by scripts/new_record.py2026-09-24T03:48:33Zcodex · EXPANDED_RECORD — Added GO respiratory-chain parentage, GO synonymy and molecular function, three reviewed-label-only Sdh component rows, an E. coli PDB:1NEK canonical example, literature/PDB evidence, a compact complex II function graph, and a component-grounding TODO.2026-09-24T03:49:07Zcodex · REVISED_GRAPH — Retyped the terminal function edge so complete respiratory complex II, not the SdhCD membrane anchor alone, enables GO:0008177.2026-09-24T03:58:25Zcodex · NARROWED_GRAPH_EDGE — Weakened the SdhCD-to-quinone graph edge from quinone-pool reduction to quinone-site binding and cited both PDB:1NEK and Yankovskaya et al. 2003 for the membrane-anchor quinone site.2026-09-24T04:00:33Zcodex · NARROWED_GRAPH_EDGE — Retyped the quinone-side graph node from a generic pool to bound ubiquinone Q2 and narrowed the SdhCD edge predicate to ligand binding.
Source: data/structures/energy_complex/respiratory_chain_complex_ii_succinate_dehydrogenase.yaml