Oxidative phosphorylation (OXPHOS) module

A taxon-neutral decomposition of oxidative phosphorylation: the coupled process by which a respiratory electron transport chain (ETC) oxidizes reduced cofactors and uses the released free energy to pump protons across a coupling membrane, and an F1Fo-ATP synthase uses the resulting proton-motive force to phosphorylate ADP. The module is deliberately phrased in terms of functional modules, protein complexes, and pathway segments rather than a fixed gene list, so it can represent the mitochondrial inner-membrane chain of eukaryotes and the plasma-membrane respiratory chains of aerobic bacteria. Design intent for complexes (the central modelling question): each respiratory complex is represented as a single PROTEIN_COMPLEX node whose emergent, complex-level catalytic activity is carried by ONE complex-level annoton (the redox half-reaction it performs), with its functionally important subunits exposed as `active_units` on the complex descriptor rather than as separate per-subunit annotons. This mirrors the GO `contributes_to` philosophy: an individual subunit contributes to but does not independently enable the complex activity. Large, internally modular complexes (Complex I; the F1Fo-ATP synthase) are additionally decomposed with `parts` into their functional sub-modules (the N/Q/proton-pumping arms of Complex I; the F1 catalytic head and Fo proton turbine of ATP synthase) — this recursive decomposition is the payoff of the module representation over a flat subunit list. Lineage- and chemistry-specific alternatives that bypass the proton-pumping complexes (type-II NADH dehydrogenase, the alternative oxidase, bacterial bd-type oxidases) are captured as `variant_sets` along explicit axes, so OXPHOS reads as one conserved energy-conservation plan with multiple implementations. Complex assembly/biogenesis is treated as a distinct process from chain operation and kept as an optional sub-module.

MODULE:oxidative_phosphorylationDRAFTBiological Processmodules/oxphos.yaml
oxidative phosphorylationGO:0006119 aerobic respirationGO:0009060 generation of precursor metabolites and energyGO:0006091
GO:0006119
oxidative phosphorylation
The module is grounded in the GO biological-process term for oxidative phosphorylation.
GO:0022904
respiratory electron transport chain
Grounds the electron-transport-chain sub-process that builds the proton-motive force.
GO:0042776
proton motive force-driven mitochondrial ATP synthesis
Grounds the chemiosmotic ATP-synthesis sub-process coupled to the ETC.
PMID:31911585
Mitochondrial TCA Cycle and OXPHOS metabolism
Review establishing the coordination of the TCA cycle and OXPHOS and the role of Complex II (succinate dehydrogenase) as the shared node feeding electrons from the TCA cycle into the respiratory chain.
file:projects/OXPHOS.md
OXPHOS project page
The sibling gene-by-gene OXPHOS curation project, which this module generalizes from concrete human subunits and assembly factors to a taxon-neutral, recursively decomposable plan.

Identifiers are grounded only where verified against the local validated OXPHOS gene reviews, the OXPHOS project page, or the sibling photosynthesis module; descriptors without a `term` are deliberate (no confident identifier yet, or no exact GO term exists for the abstraction) rather than oversights. Subunit `active_units` are named by their conserved subunit/homolog families (human gene-symbol families given as orienting names) to keep the module taxon-neutral; a concrete organism module can later specialize these with specific UniProt gene products, stoichiometries, and compartments without the generic module enumerating every protein. Complex II is intentionally modelled here as a respiratory-chain electron-entry complex; its succinate->fumarate half-reaction simultaneously belongs to the TCA cycle and is the canonical dual-pathway node. The plasma membrane substitutes for the mitochondrial inner membrane as the coupling membrane in respiring bacteria. Scope boundaries: the biosynthesis of the quinone pool (e.g. the ubiquinone/CoQ COQ pathway) and of the redox cofactors (heme a/b/c, Fe-S clusters, FAD/FMN, copper centres), as well as the pro-apoptotic role of cytochrome c once released to the cytosol, are upstream or downstream of OXPHOS operation and are intentionally out of scope here; they belong to their own pathways/gene reviews, and this module treats the carriers and cofactors as supplied inputs. Per-complex assembly factors are given by example in the biogenesis sub-module rather than broken out as structured per-complex annotons; a concrete organism-specific specialization can add that detail.

24Nodes
18Parts
2Variant Sets
5Variants
23Annotons
9Connections

Derived QC

Recommended-field compliance

100.0% recommended fields populated

All recommended fields populated.

Module deep research

✗ none found

No MODULE:oxidative_phosphorylation deep-research report alongside the module YAML.

Template conformance

every declared conforms_to bundle matches its template motif.

Gene-review completeness (0/0 grounded genes reviewed)

No concrete UniProt-grounded genes in this module.

Details

Context
aerobic (and facultative) bacteria mitochondriate eukaryotes
mitochondrial inner membrane (eukaryotes)GO:0005743 plasma membrane (respiring bacteria)
Oxidative phosphorylationBiological Processoxidative_phosphorylation
oxidative phosphorylationGO:0006119 aerobic respirationGO:0009060 generation of precursor metabolites and energyGO:0006091
Context
aerobic (and facultative) bacteria mitochondriate eukaryotes
mitochondrial inner membrane (eukaryotes)GO:0005743 plasma membrane (respiring bacteria)

Connections

The electron transport chain pumps protons to build the proton-motive force that the ATP synthase consumes. This is energetic (chemiosmotic) coupling across the membrane, not a direct metabolite hand-off; the two are obligately coupled but can be uncoupled (e.g. by uncoupling proteins or protonophores).
Part 1: respiratory electron transport and proton pumping
Respiratory electron transport chainBiological Processrespiratory_etc

Sequential, exergonic electron transfer from reduced cofactors to a terminal acceptor through membrane redox complexes and two mobile carriers (a quinone pool and a soluble cytochrome/copper carrier), with three of the canonical complexes (I, III, IV) coupling electron flow to vectorial proton translocation that charges the membrane.

respiratory electron transport chainGO:0022904 electron transport chainGO:0022900

Connections

complex_I -> quinone_pool Provides Input For
Complex I reduces ubiquinone to ubiquinol, charging the quinone pool.
complex_II -> quinone_pool Provides Input For
Complex II reduces the quinone pool from succinate (TCA cycle).
ETF-QO, glycerol-3-phosphate dehydrogenase, and DHODH reduce the quinone pool from other pathways.
quinone_pool -> complex_III Provides Input For
Ubiquinol from the pool is the substrate oxidized by Complex III at the Qo site.
complex_III -> cytochrome_c Provides Input For
Complex III reduces the soluble cytochrome c carrier.
cytochrome_c -> complex_IV Provides Input For
Reduced cytochrome c donates electrons to Complex IV.
The alternative oxidase and bacterial quinol oxidases draw electrons directly from the quinone pool, bypassing CIII/CIV.
Part 1: NADH:quinone oxidoreduction (canonical, proton-pumping)
Complex I (NADH:ubiquinone oxidoreductase)Protein Complexcomplex_I

The largest respiratory complex (~1 MDa; ~14 conserved core subunits plus many accessory subunits in eukaryotes). An L-shaped enzyme whose hydrophilic arm oxidizes NADH and relays electrons through a chain of iron-sulfur clusters to reduce ubiquinone at the arm/membrane junction, and whose membrane arm uses the redox free energy to pump four protons per NADH via antiporter-like subunits. Functionally and evolutionarily tripartite: the N (NADH-oxidizing), Q (quinone-reducing) and P (proton-pumping) modules.

respiratory chain complex IGO:0045271

Annotons

NADH:ubiquinone oxidoreductase (proton-pumping)
complex_I_activity
Participant: Protein Complex: NADH:ubiquinone oxidoreductase complex
Protein Complex:
NADH:ubiquinone oxidoreductase complexGO:0045271
Active units:
FMN/NADH-binding catalytic subunit (NDUFV1/NuoF/Nqo1 family)
Participant: Family: NDUFV1 / NuoF / Nqo1 flavoprotein family
Family:
NDUFV1 / NuoF / Nqo1 flavoprotein family
Role: Primary electron acceptor; oxidizes NADH at the FMN, the entry point of the N-module.
Function:
NADH dehydrogenase activity (FMN-dependent)GO:0003954
Iron-sulfur relay subunits (NDUFS1/NDUFV2/NDUFS7/NDUFS8 families)
Participant: Family: Complex I iron-sulfur subunits (NDUFS1/NuoG, NDUFV2/NuoE, NDUFS7/NuoB, NDUFS8/NuoI)
Family:
Complex I iron-sulfur subunits (NDUFS1/NuoG, NDUFV2/NuoE, NDUFS7/NuoB, NDUFS8/NuoI)
Role: Chain of [2Fe-2S]/[4Fe-4S] clusters conducting electrons from FMN to the quinone site.
Function:
electron transfer via iron-sulfur clustersGO:0009055
Quinone-binding core subunit (NDUFS2/NuoD/Nqo4 family)
Participant: Family: NDUFS2 / NuoD / Nqo4 family
Family:
NDUFS2 / NuoD / Nqo4 family
Role: Forms the ubiquinone-reduction site at the junction of the hydrophilic and membrane arms.
Antiporter-like proton-pumping membrane subunits (ND2/ND4/ND5; NuoL/M/N)
Participant: Family: ND2/ND4/ND5 (NuoL/NuoM/NuoN) antiporter-like family
Family:
ND2/ND4/ND5 (NuoL/NuoM/NuoN) antiporter-like family
Role: Mitochondrially (or operon)-encoded membrane subunits that translocate protons driven by quinone-coupled conformational changes.

Function

NADH:ubiquinone oxidoreductase activityGO:0008137
Substrates: NADH ubiquinone proton (matrix/cytoplasmic side)
Products: NAD+ ubiquinol proton (intermembrane/periplasmic side)
Cofactors: FMN iron-sulfur clusters

Processes

mitochondrial electron transport, NADH to ubiquinoneGO:0006120

Locations

mitochondrial inner / bacterial plasma membraneGO:0005743

Couples NADH oxidation and ubiquinone reduction to the translocation of ~4 H+ per NADH; the major entry point of electrons into the chain and a principal site of the proton-motive force and of superoxide production.

Part 1: NADH oxidation (N-module)
Complex I N-module (NADH dehydrogenase)Molecular Functioncomplex_I_N_module

Distal tip of the hydrophilic arm bearing the FMN and the first iron-sulfur clusters; oxidizes NADH and injects electrons into the relay.

Annotons

FMN-dependent NADH oxidation
ci_n_module_nadh_oxidation
Participant: Family: N-module subunits (NDUFV1/NDUFV2/NDUFS1)
Family:
N-module subunits (NDUFV1/NDUFV2/NDUFS1)

Function

NADH dehydrogenase activityGO:0003954
Substrates: NADH
Products: NAD+
Cofactors: FMN
Part 2: ubiquinone reduction (Q-module)
Complex I Q-module (quinone reduction)Molecular Functioncomplex_I_Q_module

Proximal hydrophilic-arm/membrane junction carrying the terminal iron-sulfur cluster (N2) and the ubiquinone-binding cavity where electrons reduce ubiquinone to ubiquinol.

Annotons

Ubiquinone reduction at the Q-site
ci_q_module_quinone_reduction
Participant: Family: Q-module subunits (NDUFS2/NDUFS3/NDUFS7/NDUFS8)
Family:
Q-module subunits (NDUFS2/NDUFS3/NDUFS7/NDUFS8)

Function

ubiquinone reduction Two-electron reduction of ubiquinone to ubiquinol; modelled as a sub-function of the complex-level NADH:ubiquinone oxidoreductase activity, so no separate exact GO MF id is asserted here.
Substrates: ubiquinone
Products: ubiquinol
Part 3: proton translocation (P-module / membrane arm)
Complex I P-module (membrane proton-pumping arm)Transport Stepcomplex_I_P_module

Membrane arm of antiporter-like subunits that translocate protons; conformational energy from quinone chemistry is transmitted along the arm to drive pumping remote from the redox centres.

Annotons

Redox-coupled proton translocation
ci_p_module_proton_pumping
Participant: Family: Membrane-arm antiporter-like subunits (ND1-ND6, ND4L; NuoH/J/K/L/M/N/A)
Family:
Membrane-arm antiporter-like subunits (ND1-ND6, ND4L; NuoH/J/K/L/M/N/A)

Function

proton transmembrane transportGO:1902600
Substrates: proton (matrix/cytoplasmic side)
Products: proton (intermembrane/periplasmic side)
Part 2: succinate:quinone oxidoreduction (TCA-cycle-linked, non-pumping)
Complex II (succinate dehydrogenase / succinate:quinone oxidoreductase)Protein Complexcomplex_II

The only membrane respiratory complex shared with the TCA cycle and the only canonical complex that does not pump protons. Its FAD-bearing flavoprotein oxidizes succinate to fumarate (TCA step 6) and relays electrons through three iron-sulfur clusters and a membrane b-heme to reduce ubiquinone, feeding the quinone pool without contributing to the proton-motive force.

respiratory chain complex II (succinate dehydrogenase)GO:0045273

Annotons

Succinate:ubiquinone oxidoreductase
complex_II_activity
Participant: Protein Complex: succinate dehydrogenase (ubiquinone) complex
Protein Complex:
succinate dehydrogenase (ubiquinone) complexGO:0045273
Active units:
Flavoprotein subunit (SDHA/SdhA family)
Participant: Family: SDHA / SdhA flavoprotein family
Family:
SDHA / SdhA flavoprotein family
Role: Covalent-FAD subunit; oxidizes succinate to fumarate (the TCA-cycle half-reaction).
Function:
succinate dehydrogenase activityGO:0000104
Iron-sulfur subunit (SDHB/SdhB family)
Participant: Family: SDHB / SdhB iron-sulfur family
Family:
SDHB / SdhB iron-sulfur family
Role: Three Fe-S clusters relaying electrons from FAD toward the quinone site; tumour-suppressor subunit in humans.
Function:
electron transfer activityGO:0009055
Membrane-anchor / quinone-binding subunits (SDHC+SDHD / SdhC+SdhD)
Participant: Family: SDHC/SDHD (SdhC/SdhD) membrane-anchor family
Family:
SDHC/SDHD (SdhC/SdhD) membrane-anchor family
Role: Bind heme b and form the ubiquinone-reduction site that delivers electrons to the quinone pool.

Function

succinate dehydrogenase (quinone) activityGO:0008177
Substrates: succinate ubiquinone
Products: fumarate ubiquinol
Cofactors: FAD iron-sulfur clusters heme b

Processes

mitochondrial electron transport, succinate to ubiquinoneGO:0006121

Locations

mitochondrial inner / bacterial plasma membraneGO:0005743

Bridges the TCA cycle and the respiratory chain; does not pump protons, so its electrons enter the quinone pool at no direct energetic gain to the proton-motive force.

PMID:31911585
Succinate dehydrogenase is the shared node coupling the TCA cycle to the respiratory chain.
Part 3: auxiliary quinone-reducing dehydrogenases (additional electron entry) (optional)
Auxiliary dehydrogenases feeding the quinone poolBiological Processauxiliary_quinone_dehydrogenases

Membrane-associated dehydrogenases that reduce the quinone pool outside of Complexes I/II, coupling other metabolic pathways to respiration. None pump protons. Present to varying degrees across taxa and tissues.

Annotons

Electron-transfer-flavoprotein:ubiquinone oxidoreductase (ETF-QO)
etf_quinone_oxidoreductase
Participant: Any With Function: electron-transferring-flavoprotein dehydrogenase activity
Required Function:
electron-transferring-flavoprotein dehydrogenase activityGO:0004174

Function

electron-transferring-flavoprotein dehydrogenase activityGO:0004174
Substrates: reduced electron-transfer flavoprotein ubiquinone
Products: oxidized electron-transfer flavoprotein ubiquinol

Channels electrons from mitochondrial fatty-acid beta-oxidation and amino-acid catabolism into the quinone pool.

Mitochondrial glycerol-3-phosphate dehydrogenase (FAD)
glycerol_3_phosphate_dehydrogenase
Participant: Family: FAD-dependent glycerol-3-phosphate dehydrogenase (GPD2 family)
Family:
FAD-dependent glycerol-3-phosphate dehydrogenase (GPD2 family)

Function

glycerol-3-phosphate:quinone oxidoreductase activity FAD-linked, outer-face inner-membrane enzyme of the glycerophosphate shuttle that oxidizes glycerol-3-phosphate and reduces ubiquinone; no confident exact GO MF id asserted here.
Substrates: sn-glycerol 3-phosphate ubiquinone
Products: dihydroxyacetone phosphate ubiquinol
Dihydroorotate dehydrogenase (quinone)
dihydroorotate_dehydrogenase
Participant: Any With Function: dihydroorotate dehydrogenase activity
Required Function:
dihydroorotate dehydrogenase activityGO:0004152

Function

dihydroorotate dehydrogenase (quinone) activityGO:0004152
Substrates: dihydroorotate ubiquinone
Products: orotate ubiquinol

Couples de novo pyrimidine biosynthesis to the quinone pool; a major reason respiration is required for nucleotide synthesis.

Part 4: mobile electron carrier (quinone pool)
Quinone pool (ubiquinone/menaquinone)Molecular Functionquinone_pool

Lipid-soluble two-electron/two-proton carrier diffusing within the membrane that collects electrons from all upstream dehydrogenases and delivers them to Complex III (or to a quinol oxidase). The quinone used is lineage-dependent.

Annotons

Membrane quinone electron/proton carrier
quinone_electron_carrier
Participant: Any Participant: A diffusible membrane quinone (not a protein); represented as a functional carrier node.
A diffusible membrane quinone (not a protein); represented as a functional carrier node.

Function

quinone-mediated electron and proton transferGO:0009055
Cofactors: ubiquinone (CoQ10) — most eukaryotes and many proteobacteria menaquinone / demethylmenaquinone — many bacteria

Locations

mitochondrial inner / bacterial plasma membrane (lipid bilayer)GO:0005743
Part 5: quinol:cytochrome-c oxidoreduction (canonical, proton-pumping)
Complex III (cytochrome bc1 / quinol:cytochrome-c reductase)Protein Complexcomplex_III

An obligate homodimer that oxidizes ubiquinol and reduces the soluble carrier (cytochrome c / c2) via the protonmotive Q-cycle, in which bifurcated electron transfer recycles one electron through two b-hemes to a second quinone, doubling the protons translocated per electron reaching cytochrome c.

respiratory chain complex IIIGO:0045275

Annotons

Quinol:cytochrome-c reductase (Q-cycle)
complex_III_activity
Participant: Protein Complex: cytochrome bc1 complex (dimeric)
Protein Complex:
cytochrome bc1 complex (dimeric)GO:0045275
Active units:
Cytochrome b (MT-CYB / PetB family)
Participant: Family: cytochrome b (MT-CYB / QcrB) family
Family:
cytochrome b (MT-CYB / QcrB) family
Role: Bears the low- and high-potential b-hemes (bL/bH) that carry out Q-cycle electron bifurcation; the only mtDNA-encoded subunit in animals.
Function:
electron transfer via b-type hemesGO:0009055
Cytochrome c1 (CYC1 family)
Participant: Family: cytochrome c1 (CYC1 / QcrC) family
Family:
cytochrome c1 (CYC1 / QcrC) family
Role: High-potential c1 heme that reduces the soluble cytochrome c carrier.
Function:
electron transfer to cytochrome cGO:0009055
Rieske iron-sulfur protein (UQCRFS1 / PetA family)
Participant: Family: Rieske Fe-S protein (UQCRFS1 / QcrA / PetA) family
Family:
Rieske Fe-S protein (UQCRFS1 / QcrA / PetA) family
Role: Mobile [2Fe-2S] head that oxidizes ubiquinol at the Qo site and initiates Q-cycle bifurcation.
Function:
ubiquinol oxidation via [2Fe-2S] clusterGO:0009055

Function

quinol-cytochrome-c reductase activityGO:0008121
Substrates: ubiquinol cytochrome c (oxidized) proton (matrix/cytoplasmic side)
Products: ubiquinone cytochrome c (reduced) proton (intermembrane/periplasmic side)

Processes

mitochondrial electron transport, ubiquinol to cytochrome cGO:0006122

Locations

mitochondrial inner / bacterial plasma membraneGO:0005743

Oxidizes ubiquinol and reduces cytochrome c while translocating protons via the Q-cycle; frequently a rate-controlling step and a site of superoxide generation.

Part 6: mobile electron carrier (soluble cytochrome)
Cytochrome c (soluble carrier)Molecular Functioncytochrome_c

Small soluble c-type cytochrome on the positive (intermembrane space / periplasmic) face that shuttles single electrons from Complex III to Complex IV. In eukaryotes the same protein is a pro-apoptotic signal when released to the cytosol.

Annotons

Cytochrome c electron shuttling
cytochrome_c_electron_transfer
Participant: Family: cytochrome c / cytochrome c2 family
Family:
cytochrome c / cytochrome c2 family

Function

electron transfer activityGO:0009055
Cofactors: heme c

Locations

intermembrane space / periplasm (positive membrane face)GO:0005758
Part 7: terminal electron transfer to dioxygen (canonical, proton-pumping)
Complex IV (cytochrome c oxidase)Protein Complexcomplex_IV

The terminal oxidase of the canonical chain; an aa3-type heme-copper oxidase that accepts electrons from cytochrome c and reduces O2 to water at a binuclear heme a3/CuB centre, both consuming matrix protons for chemistry and pumping additional protons across the membrane.

respiratory chain complex IVGO:0045277

Annotons

Cytochrome c oxidase (O2 reduction)
complex_IV_activity
Participant: Protein Complex: cytochrome c oxidase (aa3-type)
Protein Complex:
cytochrome c oxidase (aa3-type)GO:0045277
Active units:
Catalytic subunit I (MT-CO1 / CoxA family)
Participant: Family: cytochrome c oxidase subunit I (MT-CO1 / CoxA) family
Family:
cytochrome c oxidase subunit I (MT-CO1 / CoxA) family
Role: Bears heme a, and the heme a3/CuB binuclear centre where O2 is reduced to water; contains the proton channels.
Function:
dioxygen reduction at the heme-copper centreGO:0004129
Subunit II (MT-CO2 / CoxB family)
Participant: Family: cytochrome c oxidase subunit II (MT-CO2 / CoxB) family
Family:
cytochrome c oxidase subunit II (MT-CO2 / CoxB) family
Role: Bears the binuclear CuA centre that receives electrons from cytochrome c.
Function:
electron acceptance from cytochrome c (CuA centre)GO:0009055
Subunit III (MT-CO3 / CoxC family)
Participant: Family: cytochrome c oxidase subunit III (MT-CO3 / CoxC) family
Family:
cytochrome c oxidase subunit III (MT-CO3 / CoxC) family
Role: Core membrane subunit important for assembly and proton-pathway integrity; no redox cofactor.

Function

cytochrome-c oxidase activityGO:0004129
Substrates: cytochrome c (reduced) dioxygen proton (matrix/cytoplasmic side)
Products: cytochrome c (oxidized) water proton (intermembrane/periplasmic side)
Cofactors: heme a heme a3 CuA CuB

Processes

mitochondrial electron transport, cytochrome c to oxygenGO:0006123

Locations

mitochondrial inner / bacterial plasma membraneGO:0005743

Terminal, essentially irreversible step that reduces O2 to water and pumps protons; sets the directionality of the chain and is a key regulatory and tissue-specific (isoform) node.

Part 8: lineage-specific respiratory-chain variants (bypass branches) (optional)
Lineage-specific entry and terminal-oxidase variantsBiological Processrespiratory_chain_variants

Alternative implementations of the chain that exist alongside or in place of the canonical proton-pumping complexes. These bypass branches conserve less (or no) free energy as proton-motive force but provide metabolic flexibility, stress tolerance, and redox balancing.

Variant set: NADH:quinone oxidoreduction route by enzyme family / energy conservation (One Or More)
Proton-pumping Complex IProtein Complexcanonical_complex_I_variant

The canonical, energy-conserving NADH:ubiquinone oxidoreductase (see complex_I node).

Annotons

Complex I (energy-conserving)
canonical_ci_ref
Participant: Protein Complex: respiratory chain complex I
Protein Complex:
respiratory chain complex IGO:0045271

Pumps ~4 H+ per NADH; present in most mitochondria and many bacteria.

Type-II NADH dehydrogenase (NDH-2, non-pumping)Molecular Functiontype_II_ndh_variant

Single-subunit, FAD-dependent, rotenone-insensitive alternative NADH:quinone oxidoreductase found in plants, fungi, protists, and many bacteria (and absent in mammals). It reduces the quinone pool without pumping protons, providing a non-energy-conserving NADH bypass.

Annotons

NDH-2 NADH:quinone oxidoreductase (non-pumping)
ndh2_activity
Participant: Family: type-II NADH dehydrogenase (NDH-2 / NDI1 / Ndh) family
Family:
type-II NADH dehydrogenase (NDH-2 / NDI1 / Ndh) family

Function

NADH dehydrogenase activity (non-proton-pumping)GO:0003954
Substrates: NADH quinone
Products: NAD+ quinol

Re-oxidizes NADH and reduces the quinone pool with no charge separation.

Variant set: Route from the quinone pool / cytochrome c to O2 by terminal oxidase family / energy conservation (One Or More)
Cytochrome pathway (Complex III -> cytochrome c -> Complex IV)Biological Processcytochrome_pathway_variant

The canonical, proton-pumping bc1 -> cytochrome c -> aa3 oxidase route (see complex_III, cytochrome_c, complex_IV nodes).

Annotons

bc1 / cytochrome c / aa3 oxidase route
cytochrome_pathway_ref
Participant: Protein Complex: cytochrome pathway terminal segment
Protein Complex:
cytochrome pathway terminal segment The canonical CIII + cytochrome c + CIV segment of the chain.

Energy-conserving; both CIII and CIV pump protons.

Alternative oxidase (AOX) ubiquinol:O2 bypassMolecular Functionalternative_oxidase_variant

Cyanide-insensitive, non-proton-pumping di-iron ubiquinol oxidase of plants, fungi, and many protists (and some animals) that oxidizes ubiquinol and reduces O2 to water directly, bypassing both Complex III and Complex IV and dissipating the redox energy as heat.

Annotons

Alternative oxidase (ubiquinol:O2 oxidoreductase)
aox_activity
Participant: Family: alternative oxidase (AOX) family
Family:
alternative oxidase (AOX) family

Function

ubiquinol:oxygen oxidoreductase activity (non-pumping) Reduces O2 to water using ubiquinol at a non-heme di-iron centre; no proton pumping. No confident exact GO MF id is asserted here for the generic module.
Substrates: ubiquinol dioxygen
Products: ubiquinone water

Provides an overflow/antioxidant electron sink; thermogenic in some plants.

Bacterial bd-type quinol oxidaseMolecular Functionbd_oxidase_variant

High-O2-affinity cytochrome bd quinol oxidase used by many bacteria under microaerobic or stress conditions; oxidizes quinol and reduces O2 to water with a lower (or no) proton pumping stoichiometry than heme-copper oxidases.

Annotons

Cytochrome bd quinol oxidase
bd_oxidase_activity
Participant: Family: cytochrome bd ubiquinol oxidase (CydAB) family
Family:
cytochrome bd ubiquinol oxidase (CydAB) family

Function

quinol:oxygen oxidoreductase activity Reduces O2 to water from quinol; no confident exact GO MF id asserted here for the generic module.
Substrates: quinol dioxygen
Products: quinone water

Confers tolerance to low O2, nitrosative and oxidative stress in bacteria.

Part 2: chemiosmotic ATP synthesis from the proton-motive force
ATP synthesis (F1Fo-ATP synthase, Complex V)Protein Complexatp_synthesis

A rotary molecular motor that couples proton flow down the electrochemical gradient (through the membrane Fo sector) to mechanical rotation that drives ADP phosphorylation at the catalytic F1 head. It is the terminal energy-conserving step of OXPHOS and runs reversibly: under collapse of the proton-motive force it can hydrolyze ATP, a mode restrained by a dedicated inhibitor.

proton-transporting ATP synthase complexGO:0045259 proton-transporting two-sector ATPase complexGO:0016469

Annotons

Proton-motive-force-driven ATP synthesis (rotational)
complex_V_activity
Participant: Protein Complex: F1Fo-ATP synthase
Protein Complex:
F1Fo-ATP synthaseGO:0045259
Active units:
F1 catalytic subunits (alpha3/beta3 + central stalk)
Participant: Family: F1 ATP synthase subunits (ATP5F1A/ATP5F1B/ATP5F1C; AtpA/AtpD/AtpG)
Family:
F1 ATP synthase subunits (ATP5F1A/ATP5F1B/ATP5F1C; AtpA/AtpD/AtpG)
Role: alpha3beta3 hexamer with catalytic sites on the beta subunits; the gamma/delta/epsilon central stalk converts c-ring rotation into catalytic conformational cycling.
Function:
ATP synthesis at the catalytic beta subunitGO:0046933
Fo proton-translocating sector (c-ring + a-subunit)
Participant: Family: Fo c-ring and a-subunit (ATP5MC1-3 / ATP5MK; AtpE/AtpB)
Family:
Fo c-ring and a-subunit (ATP5MC1-3 / ATP5MK; AtpE/AtpB)
Role: The membrane c-ring rotor and stator a-subunit form the two half-channels through which protons cross, driving rotation.
Function:
proton transmembrane transport coupled to rotationGO:1902600
Peripheral stalk / stator (OSCP, b, d, F6)
Participant: Family: ATP synthase peripheral stalk (ATP5PO/OSCP, ATP5PB, ATP5PD, ATP5PF; AtpF/AtpH)
Family:
ATP synthase peripheral stalk (ATP5PO/OSCP, ATP5PB, ATP5PD, ATP5PF; AtpF/AtpH)
Role: Holds the alpha3beta3 head against the torque of rotation (the stator), coupling proton flow to catalysis.

Function

proton-transporting ATP synthase activity, rotational mechanismGO:0046933
Substrates: ADP phosphate proton (intermembrane/periplasmic side)
Products: ATP proton (matrix/cytoplasmic side)

Processes

proton motive force-driven mitochondrial ATP synthesisGO:0042776

Locations

mitochondrial inner / bacterial plasma membraneGO:0005743

Converts the proton-motive force into the bulk of cellular ATP; also shapes inner-membrane cristae through dimer rows.

Part 1: catalytic head (F1)
F1 catalytic headMolecular Functionatp_synthase_F1

Soluble alpha3beta3 hexamer with three catalytic sites cycling through open/loose/tight states (binding-change mechanism) as the central stalk rotates; synthesizes ATP from ADP and phosphate.

Annotons

Rotational ATP synthesis at F1
f1_atp_synthesis
Participant: Family: F1 alpha/beta/gamma subunits
Family:
F1 alpha/beta/gamma subunits

Function

proton-transporting ATP synthase activity, rotational mechanismGO:0046933
Substrates: ADP phosphate
Products: ATP
Part 2: proton turbine (Fo)
Fo proton-translocating sectorTransport Stepatp_synthase_Fo

Membrane sector where protons crossing between the a-subunit half-channels protonate/deprotonate c-ring carboxylates, driving rotation of the c-ring and central stalk.

Annotons

Proton-driven c-ring rotation
fo_proton_transport
Participant: Family: Fo c-ring and a-subunit
Family:
Fo c-ring and a-subunit

Function

proton transmembrane transportGO:1902600
Substrates: proton (intermembrane/periplasmic side)
Products: proton (matrix/cytoplasmic side)
Part 3: inhibition of reverse (ATP-hydrolysis) mode (optional)
IF1-mediated inhibition of ATP hydrolysisRegulatory Stepatp_synthase_inhibition

A pH-sensitive inhibitor (IF1 / ATPIF1 in animals; equivalents elsewhere) binds the F1 catalytic interface when the membrane potential collapses, blocking wasteful ATP hydrolysis without impeding synthesis.

Annotons

ATP synthase inhibitory factor
if1_inhibitor
Participant: Family: ATPase inhibitory factor 1 (ATP5IF1 / IF1) family
Family:
ATPase inhibitory factor 1 (ATP5IF1 / IF1) family

Function

ATPase inhibitor activity pH-dependent inhibition of the F1 ATP-hydrolysis (reverse) reaction. No exact GO MF id asserted in the generic module.

Prevents the synthase from running backwards and dissipating ATP under ischemia/uncoupling.

Connections

if1_inhibitor -> complex_V_activity Negatively Regulates
IF1 inhibits the hydrolytic (reverse) mode of the ATP synthase.
Part 3: supercomplex (respirasome) organization (optional)
Respiratory supercomplex (respirasome) organizationCellular Componentrespirasome_organization

In many eukaryotes (and some bacteria) Complexes I, III2, and IV associate into supercomplexes/respirasomes, and the ATP synthase forms cristae-shaping dimer rows. Supercomplex assembly is promoted by dedicated factors and is thought to aid stability, assembly, and possibly substrate channeling; it is a distinct higher-order organization layered on top of the individual complexes.

Annotons

Respirasome (I+III2+IV) and ATP synthase dimer organization
respirasome_assembly
Participant: Protein Complex: respiratory chain supercomplex / respirasome
Protein Complex:
respiratory chain supercomplex / respirasome Higher-order assembly of Complex I, the Complex III dimer, and Complex IV (with assembly factors such as COX7A2L/SCAF1); no single generic GO complex id is asserted here.

Organizes the individual respiratory complexes into supercomplexes and the ATP synthase into cristae-shaping rows; an organizational, not catalytic, module.

Part 4: biogenesis of the respiratory complexes (supporting context) (optional)
OXPHOS complex biogenesis (assembly factors and cofactor delivery)Biological Processoxphos_biogenesis

Each respiratory complex is built by dedicated assembly factors and cofactor-maturation enzymes that are NOT stable subunits and do NOT themselves carry out electron transport — they should be annotated to assembly/cofactor-insertion processes, not to the chain's catalytic activities. This sub-module captures that distinction generically rather than enumerating the (dozens of) factors per complex.

Annotons

Respiratory-complex assembly factors
complex_assembly_factors
Participant: Any Participant: Examples by complex (human): Complex I — NDUFAF1-8, ACAD9, TMEM126B, NUBPL (Fe-S); Complex II — SDHAF1-4 (Fe-S/FAD); Complex III — BCS1L, LYRM7, TTC19; Complex IV — SURF1, SCO1/2, COX10/COX15 (heme A), COA factors; Complex V — TMEM70, ATPAF1/2.
Examples by complex (human): Complex I — NDUFAF1-8, ACAD9, TMEM126B, NUBPL (Fe-S); Complex II — SDHAF1-4 (Fe-S/FAD); Complex III — BCS1L, LYRM7, TTC19; Complex IV — SURF1, SCO1/2, COX10/COX15 (heme A), COA factors; Complex V — TMEM70, ATPAF1/2.

Function

respiratory-complex assembly and cofactor maturation Chaperone-, scaffold-, and cofactor-insertion activities that build and mature the complexes (Fe-S cluster transfer, heme A/heme O biosynthesis, copper delivery, FAD insertion). Modelled as a process distinct from chain operation.

Distinguishes complex biogenesis from complex function; loss of an assembly factor causes a complex deficiency without the factor being part of the mature electron-transport machinery.