nitrogenase complex
A nitrogenase enzyme complex composed of tetrameric dinitrogenase and homodimeric nitrogenase reductase subcomplexes that together catalyze ATP-dependent reduction of dinitrogen to ammonia. [GO:0016610]
Components
| Component | Type | Part of / acts on | Grounding | Genes | Stoichiometry | Essential | Role |
|---|---|---|---|---|---|---|---|
| dinitrogenase | Protein complex | part of | Reviewed label only (reviewed name; no accession asserted) | ESSENTIAL | Tetrameric metal-cluster subcomplex required with nitrogenase reductase for nitrogenase activity.
| ||
| nitrogenase reductase | Protein complex | part of | Reviewed label only (reviewed name; no accession asserted) | ESSENTIAL | Homodimeric ATP-dependent reductase subcomplex required with dinitrogenase for nitrogenase activity.
|
Canonical examples
NCBITaxon:354Azotobacter vinelandii — Bacterial source of the molybdenum-iron dinitrogenase and iron-protein reductase assembly deposited as PDB:1N2C. [PDB:1N2C]
Functions
- nitrogenase activity
GO:0016163— Nitrogenase couples ATP hydrolysis and reduced-ferredoxin oxidation to reduction of dinitrogen, producing ammonium and dihydrogen.GO:0016163GO:0016163 defines nitrogenase activity as the ATP-dependent reduced-ferredoxin:dinitrogen oxidoreductase reaction.DOI:10.1038/387370a0Schindelin et al. 1997 reported an Azotobacter vinelandii nitrogenase complex stabilized in a state containing the MoFe protein and Fe protein.
Mechanism graphs
Nitrogenase couples ATP to dinitrogen reduction (FUNCTION)
The nitrogenase complex couples ATP hydrolysis and reduced-ferredoxin oxidation to dinitrogen reduction through required dinitrogenase and nitrogenase reductase subcomplexes.
| Subject | Predicate | Object | Evidence |
|---|---|---|---|
| reduced ferredoxin | donates electrons to | nitrogenase activity |
|
| ATP | is hydrolyzed by | nitrogenase activity |
|
| nitrogenase reductase | docks with | dinitrogenase |
|
| nitrogenase reductase | contributes to | nitrogenase activity |
|
| dinitrogenase | contributes to | nitrogenase activity |
|
| dinitrogen | accepts electrons in | nitrogenase activity |
|
| nitrogenase activity | produces | ammonium |
|
| nitrogenase activity | produces | dihydrogen |
|
Discussions
- CURATION_TODO (OPEN): Resolve variant-specific Mo-Fe, V-Fe, and Fe-Fe dinitrogenase and reductase groundings before replacing the generic reviewed-label-only component rows. GO:0016610 exactly grounds the complete nitrogenase complex across multiple metal variants; the verified InterPro terms cover narrower molybdenum-iron NifD, NifK, and NifH families or broader families that also include non-nitrogenase proteins.
Evidence
GO:0016610Gene Ontology cellular-component term for the generic nitrogenase complex.GO:0140535Gene Ontology cellular-component term for intracellular protein-containing complexes.GO:1990204Gene Ontology cellular-component term for oxidoreductase complexes.GO:0016163Gene Ontology molecular-function term for nitrogenase activity.DOI:10.1038/387370a0Schindelin et al. 1997, Structure of ADP x AlF4(-)-stabilized nitrogenase complex and its implications for signal transduction, Nature.PMID:9163420PubMed identifier for Schindelin et al. 1997 as reported by the RCSB PDB:1N2C primary citation.PDB:1N2CRCSB Protein Data Bank entry for the Azotobacter vinelandii nitrogenase complex structure from Schindelin et al. 1997.
Curation history
2026-09-24T04:40:50Zcodex · CREATED_RECORD — Scaffolded by scripts/new_record.py2026-09-24T04:41:30Zcodex · EXPANDED_RECORD — Added oxidoreductase-complex parentage, reviewed-label-only dinitrogenase and nitrogenase reductase components, an Azotobacter PDB:1N2C canonical example, GO nitrogenase activity, primary Schindelin et al. literature/PDB evidence, a compact nitrogenase function graph, and a component-grounding TODO.2026-09-24T04:42:10Zcodex · NARROWED_GRAPH_EDGE — Replaced the under-supported nitrogenase reductase-to-dinitrogenase electron-transfer edge with GO:0016610-supported contribution edges from both required nitrogenase subcomplexes to nitrogenase activity.2026-09-24T04:42:50Zcodex · TIGHTENED_GRAPH_WORDING — Tightened generic nitrogenase component and graph wording to required subcomplex contribution claims and duplicated the shared GO evidence list to avoid YAML anchors.2026-09-24T04:53:24Zcodex · RESOLVED_REVIEW_ISSUE — Resolved issue #1450 by aligning the GO:0016163-backed nitrogenase activity product wording with ammonium in the function description and causal graph node/edge.
Source: data/structures/energy_complex/nitrogenase_complex.yaml