fumarate reductase complex
A membrane-bound four-subunit respiratory quinol:fumarate reductase complex whose extrinsic catalytic module and membrane-anchor module couple fumarate reduction to quinol oxidation. [GO:0045283]
Synonyms: quinol-fumarate reductase
Components
| Component | Type | Part of / acts on | Grounding | Genes | Stoichiometry | Essential | Role |
|---|---|---|---|---|---|---|---|
| Fumarate reductase, flavoprotein subunit | Protein | part of | InterPro:IPR005884 | frdA | ESSENTIAL | FAD-binding flavoprotein subunit in the membrane-extrinsic catalytic domain of the fumarate reductase complex.
| |
| fumarate reductase iron-sulfur subunit | Protein | part of | Reviewed label only (reviewed name; no accession asserted) | frdB | ESSENTIAL | Iron-sulfur subunit in the membrane-extrinsic catalytic domain that links the flavoprotein to the FrdC/FrdD membrane anchor.
| |
| Fumarate reductase, subunit C | Protein | part of | InterPro:IPR003510 | frdC | ESSENTIAL | Fifteen-kilodalton hydrophobic membrane-anchor subunit that helps link the catalytic centers of fumarate reductase to the respiratory electron-transfer chain.
| |
| Fumarate reductase, subunit D | Protein | part of | InterPro:IPR003418 | frdD | ESSENTIAL | Thirteen-kilodalton hydrophobic membrane-anchor subunit that helps anchor the fumarate reductase catalytic module to the cytoplasmic membrane.
|
Canonical examples
NCBITaxon:562Escherichia coli — Bacterial source of the four-subunit quinol:fumarate reductase structure deposited as PDB:1KF6. [PDB:1KF6]
Functions
- quinol:fumarate reductase activity — Fumarate reductase oxidizes quinol to quinone while reducing fumarate to succinate during anaerobic respiratory electron transport.
GO:0045283GO:0045283 defines fumarate reductase by the quinol-to-quinone and fumarate-to-succinate reaction opposite to respiratory complex II.DOI:10.1126/science.284.5422.1961Iverson et al. 1999 solved the structure of the E. coli fumarate reductase respiratory complex.
Mechanism graphs
Fumarate reductase couples quinol oxidation to fumarate reduction (FUNCTION)
The fumarate reductase FrdAB catalytic domain and FrdCD membrane anchor form a respiratory complex that oxidizes quinol and reduces fumarate during anaerobic electron transport.
| Subject | Predicate | Object | Evidence |
|---|---|---|---|
| fumarate reductase complex | enables | quinol:fumarate reductase activity |
|
| Fumarate reductase, flavoprotein subunit | assembles with | fumarate reductase iron-sulfur subunit |
|
| Fumarate reductase, subunit C | contributes to | fumarate reductase complex |
|
| Fumarate reductase, subunit D | contributes to | fumarate reductase complex |
|
| quinol | donates electrons to | quinol:fumarate reductase activity |
|
| fumarate | accepts electrons in | quinol:fumarate reductase activity |
|
| quinol:fumarate reductase activity | produces | quinone |
|
| quinol:fumarate reductase activity | produces | succinate |
|
Discussions
- CURATION_TODO (OPEN): Resolve an exact source-neutral protein-family identifier for fumarate reductase subunit B before replacing its reviewed-label-only component row. InterPro IPR004489 covers succinate dehydrogenase and fumarate reductase iron-sulfur proteins, so this record grounds exact FrdA, FrdC, and FrdD families while leaving FrdB ungrounded until a FrdB-specific family is verified.
Evidence
GO:0045283Gene Ontology cellular-component term for the fumarate reductase complex.GO:0098803Gene Ontology cellular-component term for respiratory-chain protein complexes.InterPro:IPR005884InterPro family for the fumarate reductase FrdA flavoprotein subunit.InterPro:IPR003510InterPro family for fumarate reductase subunit C.InterPro:IPR003418InterPro family for fumarate reductase subunit D.DOI:10.1126/science.284.5422.1961Iverson et al. 1999, Structure of the Escherichia coli Fumarate reductase respiratory complex, Science.PMID:10373108PubMed identifier for the Iverson et al. 1999 E. coli fumarate reductase respiratory-complex structure paper as reported by InterPro.DOI:10.1074/jbc.M200815200Iverson et al. 2002, Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site, Journal of Biological Chemistry.PMID:11850430PubMed identifier for Iverson et al. 2002 as reported by the RCSB PDB:1KF6 primary citation.PDB:1KF6RCSB Protein Data Bank entry for the E. coli quinol:fumarate reductase structure from Iverson et al. 2002.
Curation history
2026-09-24T05:14:44Zcodex · CREATED_RECORD — Scaffolded by scripts/new_record.py2026-09-24T05:15:37Zcodex · EXPANDED_RECORD — Added respiratory-chain parentage, FrdA/FrdB/FrdC/FrdD component rows, an E. coli PDB:1KF6 canonical example, quinol:fumarate reductase activity, GO/InterPro/DOI/PMID/PDB evidence, a compact quinol-coupling function graph, and an FrdB family-grounding TODO.2026-09-24T05:16:23Zcodex · NARROWED_GRAPH_EDGE — Narrowed FrdC and FrdD graph edges from anchoring FrdA specifically to evidence-backed constituent contributions to the complete fumarate reductase complex.2026-09-24T05:27:24Zcodex · RESOLVED_REVIEW_ISSUE — Resolved issue #1452 by adding source-attested quinol-fumarate reductase synonymy from the PDB:1KF6 primary citation title.
Source: data/structures/energy_complex/fumarate_reductase_complex.yaml