Respiratory electron transport, ATP synthesis by chemiosmotic coupling, and heat production by uncoupling proteins. (Homo sapiens)

From WikiPathways

Revision as of 09:40, 9 May 2014 by Anwesha (Talk | contribs)
Jump to: navigation, search
3, 146, 73, 1441, 5, 8-10, 1343, 143, 143, 1442, 11, 12ATPase CFSuccinate dehydrogenase flavoprotein mitochondrial matrixSuccinate dehydrogenase flavoprotein UCP FA anionUCP dimer "head-out" complex Complex I - 20 kDa subunit-4Fe-4S cluster complex Complex III - cytochrome c1-heme complex UCP dimer ATPase-ADP and Pi complex Complex I - 51 kDa subunit-FMN-4Fe-4S cluster complex ATPase complex ATPase complex cytochrome b-heme complex Cytochrome c Complex I - 39 kDa subunit-FAD cofactor UCP dimer Complex I - 42 kDa subunit-FAD cofactor mitochondrial intermembrane spaceUCP ATPase CFATPase CFComplex I - 49 kDa subunit-4Fe-4S cluster complex UCP FA anionUCP dimer "head-in" complex Cytochrome c Complex I - NADHUbiquinone oxidoreductase ATPase CFUCP dimer Succinate dehydrogenase Iron Sulphur Complex I - 23 kDa subunit-2 x 4Fe-4S cluster complex ATPase-ATP complex UCP Complex IV - Cytochrome c oxidase subunit 2-Cu complex Complex I - 75 kDa subunit-2Fe-2S cluster-4Fe- 2 x 4S cluster complex ATPase CFATPase complex ETF ETF IP sub-complex HP subcomplex UCP dimer Succinate dehydrogenase complex Succinate dehydrogenase Iron Sulphur Succinate dehydrogenase complex FP sub-complex ATPase CFCytochrome c oxidase Ubiquinol-cytochrome c reductase Complex III - Rieske protein-2Fe-2S cluster complex MT-ND3 ATP5I COX7B QH2ATPFatty Acid anion "head-out" FADH2 NDUFA3PiNDUFS2 ATP5F1 AMP UQCRC1 SDHD O2ATP5G1 NDUFA13 NDUFS3 UCP3 COX4I1 NDUFA10 FAD SDHB UQCR11 FAD UCP3 NAD+ATP5I Complex I - NADHUbiquinone oxidoreductaseLong-chain fatty acidFADH2 FADSDHA NDUFS8 MT-ND5 UQCR10 UQCRB COX6B1 NDUFS5 ETFAATP5O FAD COX6A1 Ubiquinol-cytochrome c reductaseSDHD COX7A2L MT-ND4L ATP5L CYCS NDUFS1 NDUFB4 MT-CO1 ETFB ETF CYCS MT-ATP6 ATP5O UCP dimerATP5E CoQMT-ATP6 NDUFB6 Succinate dehydrogenase complex UCP1UCP2 ATP5D Cytochrome c COX7C Fatty Acid "head-in"UCP3 SDHC MT-ND1 QH2NDUFB11 ETFAUQCRQ ATPase complexATP5J CYC1 MT-CYB SDHA CuA FADH2H2OATP NDUFA5 Pi MT-ATP8 NDUFB7 ATPase-ATP complexNDUFB5 MT-ATP8 ETFH+ATP5O ATP5L COX6CATP5A1 Fatty Acid anion "head-in"UQCRH NDUFB1 NDUFA6 UCP3 MT-ND6 ATP5G1 Fatty Acid anion "head-out"ATP5J Fatty Acid anion "head-in" Cytochrome c SDHB UQCRC2 ATP5B Succinate dehydrogenase complex MT-ND2 COX5A UQCRFS1UCP2 NDUFS7 NDUFA1 UCP dimerATP5C1 NDUFC1 ATP5A1 NDUFA8 ATP5L Purine nucleotideNDUFA9 ATP5H NDUFB3 ATP5D NDUFA4 ATP5D UCP2 NDUFV3 QH2ATP5H NDUFA2 NDUFAB1 UCP1MT-ATP6 ATP5A1 AMP ATP5F1 UCP1ATP5G1 Cytochrome c oxidaseFA anionUCP dimer "head-in" complexATP5J2 ATP5F1 NDUFC2 NDUFB10NDUFA7 ferroheme NDUFB9 ATP5B ATP5J MT-ND4 ATP5B MT-CO2 ATP5E NDUFA12 COX5B SDHC ATP5J2 NADHNDUFB8 ATP5I NDUFV1 ATP5H FMN NDUFA11 ATP5E MT-ATP8 ETFDHFatty Acid "head-out"ATPase-ADP and Pi complexUCP2 NDUFS4 CoQH+ATP5C1 ADP FA anionUCP dimer "head-out" complexH2Oferriheme ATP5J2 MT-CO3ETFB ADPNDUFS6 UCP1NDUFV2 NDUFB2 COX8A ATP5C1


Description

No description

Comments

Wikipathways-description 
Oxidation of fatty acids and pyruvate in the mitochondrial matrix yield large amounts of NADH. The respiratory electron transport chain couples the re-oxidation of this NADH to NAD+ to the export of protons from the mitochonrial matrix, generating a chemiosmotic gradient across the inner mitochondrial membrane. This gradient is used to drive the synthesis of ATP; it can also be bypassed by uncoupling proteins to generate heat, a reaction in brown fat that may be important in regulation of body temperature in newborn children.

Original Pathway at Reactome: http://www.reactome.org/PathwayBrowser/#DB=gk_current&FOCUS_SPECIES_ID=48887&FOCUS_PATHWAY_ID=163200

Try the New WikiPathways

View approved pathways at the new wikipathways.org.

Quality Tags

Ontology Terms

 

Bibliography

View all...
  1. Stanley CA, Hale DE.; ''Genetic disorders of mitochondrial fatty acid oxidation.''; PubMed Europe PMC Scholia
  2. Allan CM, Hill S, Morvaridi S, Saiki R, Johnson JS, Liau WS, Hirano K, Kawashima T, Ji Z, Loo JA, Shepherd JN, Clarke CF.; ''A conserved START domain coenzyme Q-binding polypeptide is required for efficient Q biosynthesis, respiratory electron transport, and antioxidant function in Saccharomyces cerevisiae.''; PubMed Europe PMC Scholia
  3. Yoshida S, Tsutsumi S, Muhlebach G, Sourbier C, Lee MJ, Lee S, Vartholomaiou E, Tatokoro M, Beebe K, Miyajima N, Mohney RP, Chen Y, Hasumi H, Xu W, Fukushima H, Nakamura K, Koga F, Kihara K, Trepel J, Picard D, Neckers L.; ''Molecular chaperone TRAP1 regulates a metabolic switch between mitochondrial respiration and aerobic glycolysis.''; PubMed Europe PMC Scholia
  4. Fontanesi F, Soto IC, Horn D, Barrientos A.; ''Assembly of mitochondrial cytochrome c-oxidase, a complicated and highly regulated cellular process.''; PubMed Europe PMC Scholia
  5. Boyer PD, Cross RL, Momsen W.; ''A new concept for energy coupling in oxidative phosphorylation based on a molecular explanation of the oxygen exchange reactions.''; PubMed Europe PMC Scholia
  6. Hirst J, Carroll J, Fearnley IM, Shannon RJ, Walker JE.; ''The nuclear encoded subunits of complex I from bovine heart mitochondria.''; PubMed Europe PMC Scholia
  7. Barros MH, Johnson A, Gin P, Marbois BN, Clarke CF, Tzagoloff A.; ''The Saccharomyces cerevisiae COQ10 gene encodes a START domain protein required for function of coenzyme Q in respiration.''; PubMed Europe PMC Scholia
  8. Balsa E, Marco R, Perales-Clemente E, Szklarczyk R, Calvo E, Landázuri MO, Enríquez JA.; ''NDUFA4 is a subunit of complex IV of the mammalian electron transport chain.''; PubMed Europe PMC Scholia
  9. Mitchell P.; ''Protonmotive redox mechanism of the cytochrome b-c1 complex in the respiratory chain: protonmotive ubiquinone cycle.''; PubMed Europe PMC Scholia
  10. Wikstrom MK.; ''Proton pump coupled to cytochrome c oxidase in mitochondria.''; PubMed Europe PMC Scholia
  11. Yano T.; ''The energy-transducing NADH: quinone oxidoreductase, complex I.''; PubMed Europe PMC Scholia
  12. Wood PA.; ''Defects in mitochondrial beta-oxidation of fatty acids.''; PubMed Europe PMC Scholia
  13. Loeffen J, Elpeleg O, Smeitink J, Smeets R, Stöckler-Ipsiroglu S, Mandel H, Sengers R, Trijbels F, van den Heuvel L.; ''Mutations in the complex I NDUFS2 gene of patients with cardiomyopathy and encephalomyopathy.''; PubMed Europe PMC Scholia
  14. Belogrudov GI, Hatefi Y.; ''Factor B and the mitochondrial ATP synthase complex.''; PubMed Europe PMC Scholia
  15. Rinaldo P, Matern D, Bennett MJ.; ''Fatty acid oxidation disorders.''; PubMed Europe PMC Scholia
  16. Sciacovelli M, Guzzo G, Morello V, Frezza C, Zheng L, Nannini N, Calabrese F, Laudiero G, Esposito F, Landriscina M, Defilippi P, Bernardi P, Rasola A.; ''The mitochondrial chaperone TRAP1 promotes neoplastic growth by inhibiting succinate dehydrogenase.''; PubMed Europe PMC Scholia
  17. Trumpower BL, Gennis RB.; ''Energy transduction by cytochrome complexes in mitochondrial and bacterial respiration: the enzymology of coupling electron transfer reactions to transmembrane proton translocation.''; PubMed Europe PMC Scholia
  18. Stiburek L, Hansikova H, Tesarova M, Cerna L, Zeman J.; ''Biogenesis of eukaryotic cytochrome c oxidase.''; PubMed Europe PMC Scholia
  19. Schultz BE, Chan SI.; ''Structures and proton-pumping strategies of mitochondrial respiratory enzymes.''; PubMed Europe PMC Scholia
  20. Garlid KD, Jaburek M, Jezek P.; ''Mechanism of uncoupling protein action.''; PubMed Europe PMC Scholia
  21. Belogrudov GI.; ''Factor B is essential for ATP synthesis by mitochondria.''; PubMed Europe PMC Scholia
  22. Roe CR, Roe DS.; ''Recent developments in the investigation of inherited metabolic disorders using cultured human cells.''; PubMed Europe PMC Scholia
  23. Loeffen JL, Triepels RH, van den Heuvel LP, Schuelke M, Buskens CA, Smeets RJ, Trijbels JM, Smeitink JA.; ''cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed.''; PubMed Europe PMC Scholia
  24. Long JZ, Svensson KJ, Bateman LA, Lin H, Kamenecka T, Lokurkar IA, Lou J, Rao RR, Chang MR, Jedrychowski MP, Paulo JA, Gygi SP, Griffin PR, Nomura DK, Spiegelman BM.; ''The Secreted Enzyme PM20D1 Regulates Lipidated Amino Acid Uncouplers of Mitochondria.''; PubMed Europe PMC Scholia
  25. Estornell E, Fato R, Castelluccio C, Cavazzoni M, Parenti Castelli G, Lenaz G.; ''Saturation kinetics of coenzyme Q in NADH and succinate oxidation in beef heart mitochondria.''; PubMed Europe PMC Scholia
  26. Soto IC, Fontanesi F, Liu J, Barrientos A.; ''Biogenesis and assembly of eukaryotic cytochrome c oxidase catalytic core.''; PubMed Europe PMC Scholia
  27. Echtay KS, Roussel D, St-Pierre J, Jekabsons MB, Cadenas S, Stuart JA, Harper JA, Roebuck SJ, Morrison A, Pickering S, Clapham JC, Brand MD.; ''Superoxide activates mitochondrial uncoupling proteins.''; PubMed Europe PMC Scholia
  28. Kevelam SH, Rodenburg RJ, Wolf NI, Ferreira P, Lunsing RJ, Nijtmans LG, Mitchell A, Arroyo HA, Rating D, Vanderver A, van Berkel CG, Abbink TE, Heutink P, van der Knaap MS.; ''NUBPL mutations in patients with complex I deficiency and a distinct MRI pattern.''; PubMed Europe PMC Scholia
  29. Schuelke M, Loeffen J, Mariman E, Smeitink J, van den Heuvel L.; ''Cloning of the human mitochondrial 51 kDa subunit (NDUFV1) reveals a 100% antisense homology of its 3'UTR with the 5'UTR of the gamma-interferon inducible protein (IP-30) precursor: is this a link between mitochondrial myopathy and inflammation?''; PubMed Europe PMC Scholia
  30. Garlid KD, Orosz DE, Modrianský M, Vassanelli S, Jezek P.; ''On the mechanism of fatty acid-induced proton transport by mitochondrial uncoupling protein.''; PubMed Europe PMC Scholia
  31. Pitceathly RD, Rahman S, Wedatilake Y, Polke JM, Cirak S, Foley AR, Sailer A, Hurles ME, Stalker J, Hargreaves I, Woodward CE, Sweeney MG, Muntoni F, Houlden H, Taanman JW, Hanna MG, UK10K Consortium.; ''NDUFA4 mutations underlie dysfunction of a cytochrome c oxidase subunit linked to human neurological disease.''; PubMed Europe PMC Scholia
  32. Smeitink J, Sengers R, Trijbels F, van den Heuvel L.; ''Human NADH:ubiquinone oxidoreductase.''; PubMed Europe PMC Scholia
  33. Mckenzie M, Ryan MT.; ''Assembly factors of human mitochondrial complex I and their defects in disease.''; PubMed Europe PMC Scholia
  34. Andrews B, Carroll J, Ding S, Fearnley IM, Walker JE.; ''Assembly factors for the membrane arm of human complex I.''; PubMed Europe PMC Scholia
  35. Jezek P, Hanus J, Semrad C, Garlid KD.; ''Photoactivated azido fatty acid irreversibly inhibits anion and proton transport through the mitochondrial uncoupling protein.''; PubMed Europe PMC Scholia
  36. Bourges I, Ramus C, Mousson de Camaret B, Beugnot R, Remacle C, Cardol P, Hofhaus G, Issartel JP.; ''Structural organization of mitochondrial human complex I: role of the ND4 and ND5 mitochondria-encoded subunits and interaction with prohibitin.''; PubMed Europe PMC Scholia
  37. Mimaki M, Wang X, McKenzie M, Thorburn DR, Ryan MT.; ''Understanding mitochondrial complex I assembly in health and disease.''; PubMed Europe PMC Scholia
  38. Sass JO.; ''Inborn errors of ketogenesis and ketone body utilization.''; PubMed Europe PMC Scholia
  39. Sheftel AD, Stehling O, Pierik AJ, Netz DJ, Kerscher S, Elsässer HP, Wittig I, Balk J, Brandt U, Lill R.; ''Human ind1, an iron-sulfur cluster assembly factor for respiratory complex I.''; PubMed Europe PMC Scholia
  40. Carilla-Latorre S, Gallardo ME, Annesley SJ, Calvo-Garrido J, Graña O, Accari SL, Smith PK, Valencia A, Garesse R, Fisher PR, Escalante R.; ''MidA is a putative methyltransferase that is required for mitochondrial complex I function.''; PubMed Europe PMC Scholia
  41. MacLennan DH, Lenaz G, Szarkowska L.; ''Studies on the mechanims of oxidative phosphorylation. IX. Effect of cytochrome c on energy-linked processes.''; PubMed Europe PMC Scholia
  42. Mitchell P.; ''Possible molecular mechanisms of the protonmotive function of cytochrome systems.''; PubMed Europe PMC Scholia
  43. Coates PM, Tanaka K.; ''Molecular basis of mitochondrial fatty acid oxidation defects.''; PubMed Europe PMC Scholia
  44. Echtay KS, Murphy MP, Smith RA, Talbot DA, Brand MD.; ''Superoxide activates mitochondrial uncoupling protein 2 from the matrix side. Studies using targeted antioxidants.''; PubMed Europe PMC Scholia
  45. Friedrich T, Böttcher B.; ''The gross structure of the respiratory complex I: a Lego System.''; PubMed Europe PMC Scholia
  46. Guzzo G, Sciacovelli M, Bernardi P, Rasola A.; ''Inhibition of succinate dehydrogenase by the mitochondrial chaperone TRAP1 has anti-oxidant and anti-apoptotic effects on tumor cells.''; PubMed Europe PMC Scholia

History

View all...
CompareRevisionActionTimeUserComment
114966view16:49, 25 January 2021ReactomeTeamReactome version 75
113410view11:48, 2 November 2020ReactomeTeamReactome version 74
112612view15:59, 9 October 2020ReactomeTeamReactome version 73
101528view11:39, 1 November 2018ReactomeTeamreactome version 66
101063view21:21, 31 October 2018ReactomeTeamreactome version 65
100594view19:55, 31 October 2018ReactomeTeamreactome version 64
100143view16:40, 31 October 2018ReactomeTeamreactome version 63
99693view15:09, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99281view12:45, 31 October 2018ReactomeTeamreactome version 62
93907view13:44, 16 August 2017ReactomeTeamreactome version 61
93481view11:24, 9 August 2017ReactomeTeamreactome version 61
86578view09:21, 11 July 2016ReactomeTeamreactome version 56
83426view11:11, 18 November 2015ReactomeTeamVersion54
81630view13:10, 21 August 2015ReactomeTeamVersion53
77091view08:38, 17 July 2014ReactomeTeamFixed remaining interactions
76797view12:18, 16 July 2014ReactomeTeamFixed remaining interactions
76120view10:18, 11 June 2014ReactomeTeamRe-fixing comment source
75832view11:40, 10 June 2014ReactomeTeamReactome 48 Update
75192view09:40, 9 May 2014AnweshaFixing comment source for displaying WikiPathways description
74837view10:06, 30 April 2014ReactomeTeamReactome46
74431view07:10, 19 April 2014EgonwRelocated an InfoBox.
68937view17:34, 8 July 2013MaintBotUpdated to 2013 gpml schema
45047view19:09, 6 October 2011ThomasOntology Term : 'energy metabolic pathway' added !
42118view21:58, 4 March 2011MaintBotAutomatic update
39928view05:56, 21 January 2011MaintBotNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
ADP MetaboliteCHEBI:16761 (ChEBI)
ADPMetaboliteCHEBI:16761 (ChEBI)
AMP MetaboliteCHEBI:16027 (ChEBI)
ATP MetaboliteCHEBI:15422 (ChEBI)
ATP5A1 ProteinP25705 (Uniprot-TrEMBL)
ATP5B ProteinP06576 (Uniprot-TrEMBL)
ATP5C1 ProteinP36542 (Uniprot-TrEMBL)
ATP5D ProteinP30049 (Uniprot-TrEMBL)
ATP5E ProteinP56381 (Uniprot-TrEMBL)
ATP5F1 ProteinP24539 (Uniprot-TrEMBL)
ATP5G1 ProteinP05496 (Uniprot-TrEMBL)
ATP5H ProteinO75947 (Uniprot-TrEMBL)
ATP5I ProteinP56385 (Uniprot-TrEMBL)
ATP5J ProteinP18859 (Uniprot-TrEMBL)
ATP5J2 ProteinP56134 (Uniprot-TrEMBL)
ATP5L ProteinO75964 (Uniprot-TrEMBL)
ATP5O ProteinP48047 (Uniprot-TrEMBL)
ATPMetaboliteCHEBI:15422 (ChEBI)
ATPase complexComplexREACT_4862 (Reactome)
ATPase-ADP and Pi complexComplexREACT_2435 (Reactome)
ATPase-ATP complexComplexREACT_3945 (Reactome)
COX4I1 ProteinP13073 (Uniprot-TrEMBL)
COX5A ProteinP20674 (Uniprot-TrEMBL)
COX5B ProteinP10606 (Uniprot-TrEMBL)
COX6A1 ProteinP12074 (Uniprot-TrEMBL)
COX6B1 ProteinP14854 (Uniprot-TrEMBL)
COX6CProteinP09669 (Uniprot-TrEMBL)
COX7A2L ProteinO14548 (Uniprot-TrEMBL)
COX7B ProteinP24311 (Uniprot-TrEMBL)
COX7C ProteinP15954 (Uniprot-TrEMBL)
COX8A ProteinP10176 (Uniprot-TrEMBL)
CYC1 ProteinP08574 (Uniprot-TrEMBL)
CYCS ProteinP99999 (Uniprot-TrEMBL)
CoQMetaboliteCHEBI:16389 (ChEBI)
Complex I - NADH Ubiquinone oxidoreductaseComplexREACT_6533 (Reactome)
CuA MetaboliteCHEBI:28694 (ChEBI)
Cytochrome c ComplexREACT_13858 (Reactome)
Cytochrome c ComplexREACT_13953 (Reactome)
Cytochrome c oxidaseComplexREACT_6661 (Reactome)
ETF ComplexREACT_6568 (Reactome)
ETFAProteinP13804 (Uniprot-TrEMBL)
ETFB ProteinP38117 (Uniprot-TrEMBL)
ETFDHProteinQ16134 (Uniprot-TrEMBL)
ETFComplexREACT_6490 (Reactome)
FA anion UCP dimer "head-out" complexComplexREACT_6437 (Reactome)
FA anion UCP dimer "head-in" complexComplexREACT_6679 (Reactome)
FAD MetaboliteCHEBI:16238 (ChEBI)
FADMetaboliteCHEBI:16238 (ChEBI)
FADH2 MetaboliteCHEBI:17877 (ChEBI)
FADH2MetaboliteCHEBI:17877 (ChEBI)
FMN MetaboliteCHEBI:17621 (ChEBI)
Fatty Acid "head-in"CHEBI:35366 (ChEBI)
Fatty Acid "head-out"CHEBI:35366 (ChEBI)
Fatty Acid anion "head-in" MetaboliteCHEBI:28868 (ChEBI)
Fatty Acid anion "head-in"CHEBI:28868 (ChEBI)
Fatty Acid anion "head-out" MetaboliteCHEBI:28868 (ChEBI)
Fatty Acid anion "head-out"CHEBI:28868 (ChEBI)
H+MetaboliteCHEBI:15378 (ChEBI)
H2OMetaboliteCHEBI:15377 (ChEBI)
Long-chain fatty acidCHEBI:15904 (ChEBI)
MT-ATP6 ProteinP00846 (Uniprot-TrEMBL)
MT-ATP8 ProteinP03928 (Uniprot-TrEMBL)
MT-CO1 ProteinP00395 (Uniprot-TrEMBL)
MT-CO2 ProteinP00403 (Uniprot-TrEMBL)
MT-CO3ProteinP00414 (Uniprot-TrEMBL)
MT-CYB ProteinP00156 (Uniprot-TrEMBL)
MT-ND1 ProteinP03886 (Uniprot-TrEMBL)
MT-ND2 ProteinP03891 (Uniprot-TrEMBL)
MT-ND3 ProteinP03897 (Uniprot-TrEMBL)
MT-ND4 ProteinP03905 (Uniprot-TrEMBL)
MT-ND4L ProteinP03901 (Uniprot-TrEMBL)
MT-ND5 ProteinP03915 (Uniprot-TrEMBL)
MT-ND6 ProteinP03923 (Uniprot-TrEMBL)
NAD+MetaboliteCHEBI:15846 (ChEBI)
NADHMetaboliteCHEBI:16908 (ChEBI)
NDUFA1 ProteinO15239 (Uniprot-TrEMBL)
NDUFA10 ProteinO95299 (Uniprot-TrEMBL)
NDUFA11 ProteinQ86Y39 (Uniprot-TrEMBL)
NDUFA12 ProteinQ9UI09 (Uniprot-TrEMBL)
NDUFA13 ProteinQ9P0J0 (Uniprot-TrEMBL)
NDUFA2 ProteinO43678 (Uniprot-TrEMBL)
NDUFA3ProteinO95167 (Uniprot-TrEMBL)
NDUFA4 ProteinO00483 (Uniprot-TrEMBL)
NDUFA5 ProteinQ16718 (Uniprot-TrEMBL)
NDUFA6 ProteinP56556 (Uniprot-TrEMBL)
NDUFA7 ProteinO95182 (Uniprot-TrEMBL)
NDUFA8 ProteinP51970 (Uniprot-TrEMBL)
NDUFA9 ProteinQ16795 (Uniprot-TrEMBL)
NDUFAB1 ProteinO14561 (Uniprot-TrEMBL)
NDUFB1 ProteinO75438 (Uniprot-TrEMBL)
NDUFB10ProteinO96000 (Uniprot-TrEMBL)
NDUFB11 ProteinQ9NX14 (Uniprot-TrEMBL)
NDUFB2 ProteinO95178 (Uniprot-TrEMBL)
NDUFB3 ProteinO43676 (Uniprot-TrEMBL)
NDUFB4 ProteinO95168 (Uniprot-TrEMBL)
NDUFB5 ProteinO43674 (Uniprot-TrEMBL)
NDUFB6 ProteinO95139 (Uniprot-TrEMBL)
NDUFB7 ProteinP17568 (Uniprot-TrEMBL)
NDUFB8 ProteinO95169 (Uniprot-TrEMBL)
NDUFB9 ProteinQ9Y6M9 (Uniprot-TrEMBL)
NDUFC1 ProteinO43677 (Uniprot-TrEMBL)
NDUFC2 ProteinO95298 (Uniprot-TrEMBL)
NDUFS1 ProteinP28331 (Uniprot-TrEMBL)
NDUFS2 ProteinO75306 (Uniprot-TrEMBL)
NDUFS3 ProteinO75489 (Uniprot-TrEMBL)
NDUFS4 ProteinO43181 (Uniprot-TrEMBL)
NDUFS5 ProteinO43920 (Uniprot-TrEMBL)
NDUFS6 ProteinO75380 (Uniprot-TrEMBL)
NDUFS7 ProteinO75251 (Uniprot-TrEMBL)
NDUFS8 ProteinO00217 (Uniprot-TrEMBL)
NDUFV1 ProteinP49821 (Uniprot-TrEMBL)
NDUFV2 ProteinP19404 (Uniprot-TrEMBL)
NDUFV3 ProteinP56181 (Uniprot-TrEMBL)
O2MetaboliteCHEBI:15379 (ChEBI)
Pi MetaboliteCHEBI:18367 (ChEBI)
PiMetaboliteCHEBI:18367 (ChEBI)
Purine nucleotideREACT_6384 (Reactome)
QH2MetaboliteCHEBI:17976 (ChEBI)
SDHA ProteinP31040 (Uniprot-TrEMBL)
SDHB ProteinP21912 (Uniprot-TrEMBL)
SDHC ProteinQ99643 (Uniprot-TrEMBL)
SDHD ProteinO14521 (Uniprot-TrEMBL)
Succinate dehydrogenase complex ComplexREACT_3127 (Reactome)
Succinate dehydrogenase complex ComplexREACT_6402 (Reactome)
UCP dimerComplexREACT_6463 (Reactome)
UCP1ProteinP25874 (Uniprot-TrEMBL)
UCP2 ProteinP55851 (Uniprot-TrEMBL)
UCP3 ProteinP55916 (Uniprot-TrEMBL)
UQCR10 ProteinQ9UDW1 (Uniprot-TrEMBL)
UQCR11 ProteinO14957 (Uniprot-TrEMBL)
UQCRB ProteinP14927 (Uniprot-TrEMBL)
UQCRC1 ProteinP31930 (Uniprot-TrEMBL)
UQCRC2 ProteinP22695 (Uniprot-TrEMBL)
UQCRFS1ProteinP47985 (Uniprot-TrEMBL)
UQCRH ProteinP07919 (Uniprot-TrEMBL)
UQCRQ ProteinO14949 (Uniprot-TrEMBL)
Ubiquinol-cytochrome c reductaseComplexREACT_6527 (Reactome)
ferriheme MetaboliteCHEBI:38574 (ChEBI)
ferroheme MetaboliteCHEBI:38573 (ChEBI)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
ADPREACT_991 (Reactome)
ATPArrowREACT_1985 (Reactome)
ATPase complexArrowREACT_1985 (Reactome)
ATPase complexREACT_991 (Reactome)
ATPase-ADP and Pi complexREACT_190 (Reactome)
ATPase-ATP complexArrowREACT_190 (Reactome)
ATPase-ATP complexREACT_1985 (Reactome)
CoQArrowREACT_6300 (Reactome)
CoQREACT_6169 (Reactome)
CoQREACT_6300 (Reactome)
CoQREACT_6310 (Reactome)
CoQREACT_6360 (Reactome)
Complex I - NADH Ubiquinone oxidoreductaseREACT_6310 (Reactome)
Cytochrome c ArrowREACT_6149 (Reactome)
Cytochrome c ArrowREACT_6300 (Reactome)
Cytochrome c REACT_6149 (Reactome)
Cytochrome c REACT_6300 (Reactome)
Cytochrome c oxidaseREACT_6149 (Reactome)
ETF ArrowREACT_6154 (Reactome)
ETF REACT_6169 (Reactome)
ETFArrowREACT_6169 (Reactome)
ETFDHREACT_6169 (Reactome)
ETFREACT_6154 (Reactome)
FA anion UCP dimer "head-in" complexREACT_6188 (Reactome)
FADArrowREACT_6154 (Reactome)
FADH2REACT_6154 (Reactome)
Fatty Acid anion "head-in"ArrowREACT_6302 (Reactome)
Fatty Acid anion "head-in"REACT_6165 (Reactome)
Fatty Acid anion "head-out"ArrowREACT_6218 (Reactome)
Fatty Acid anion "head-out"REACT_6205 (Reactome)
H+ArrowREACT_1985 (Reactome)
H+ArrowREACT_6149 (Reactome)
H+ArrowREACT_6300 (Reactome)
H+ArrowREACT_6302 (Reactome)
H+ArrowREACT_6310 (Reactome)
H+REACT_1985 (Reactome)
H+REACT_6149 (Reactome)
H+REACT_6205 (Reactome)
H+REACT_6300 (Reactome)
H+REACT_6310 (Reactome)
H2OArrowREACT_190 (Reactome)
H2OArrowREACT_6149 (Reactome)
Long-chain fatty acidArrowREACT_6312 (Reactome)
NAD+ArrowREACT_6310 (Reactome)
NADHREACT_6310 (Reactome)
O2REACT_6149 (Reactome)
PiREACT_991 (Reactome)
Purine nucleotideTBarREACT_6312 (Reactome)
QH2ArrowREACT_6169 (Reactome)
QH2ArrowREACT_6300 (Reactome)
QH2ArrowREACT_6310 (Reactome)
QH2ArrowREACT_6360 (Reactome)
QH2REACT_6300 (Reactome)
REACT_190 (Reactome) In the tight configuration, the beta subunit catalyzes the reaction of ADP + Pi to ATP + water. ATP is still tightly bound to the subunit at this stage.
REACT_1985 (Reactome) In the last step, the beta subunit is converted to the open form and ATP is released. Passage of protons through the Fo part causes a ring of approximately 10 subunits to rotate. This rotation in turn drives the rotation of the gamma subunits, which forms part of one of the stalks. The gamma subunit moves between the three beta subunits which are held in place by the second stalk which can be regarded as a stator. The polypeptide called OSCP connects the stator stalk to the assembly of alpha and beta subunits. It is this step that is coupled to proton translocation as energy is required to break the strong bond between ATP and the protein.


REACT_6149 (Reactome) Complex IV (cytochrome oxidase) contains the hemeprotein cytochrome a and a3. It also contains copper atoms which undergo a transition from Cu+ to Cu2+ during the transfer of electrons through the complex to molecular oxygen. A bimetallic centre containing a copper atom and a heme-linked iron protein binds oxygen after 4 electrons have been picked up. Water, the final product of oxygen reduction, is then released. Oxygen is the final electron acceptor in the respiratory chain. The overall reaction can be summed as below:
4Cyt c(red.) + 12H+in + O2 -> 4Cyt c(ox.) + 2H2O + 8H+out

Four protons are taken up from the matrix side of the membrane to form the water (scalar protons). Wikstrom (1977) suggests 4 protons are additionally transferred out from the matrix to the intermembrane space.
REACT_6151 (Reactome) At the beginning of this reaction, 1 molecule of 'Fatty Acid "head-out"' is present. At the end of this reaction, 1 molecule of 'Fatty Acid "head-in"' is present.

This reaction takes place in the 'mitochondrial inner membrane'.

REACT_6154 (Reactome) Electron transfer flavoprotein, ETF, a 63kDa heterodimer composed of alpha and beta subunit, binds one FAD and one AMP per dimer. ETF resides on the matrix face of the mitochondrial inner membrane. Reducing equivalents from the beta-oxidation of fatty acyl CoAs are transferred to ETF, reducing the ETF-bound FAD to FADH2.
REACT_6165 (Reactome) A FA anion diffuses laterally within the membrane towards UCP. The membrane potential drives the FA anion to an energy well halfway up on UCP. The electric field created by the redox-linked proton ejection drives the head group to the energy well.
REACT_6169 (Reactome) ETF-ubiquinone oxidoreductase (ETF-QO), catalyzes the re-oxidation of reduced ETF, with ubiquinone as the electron acceptor.
REACT_6188 (Reactome) The FA anion which was facing the matrix side of the inner mitochondrial membrane now flip-flops over to the intermembrane space-side of the membrane.
REACT_6205 (Reactome) At the beginning of this reaction, 1 molecule of 'H+', and 1 molecule of 'Fatty Acid anion "head-out"' are present. At the end of this reaction, 1 molecule of 'Fatty Acid "head-out"' is present.

This reaction takes place in the 'mitochondrial inner membrane'.

REACT_6218 (Reactome) At the beginning of this reaction, 1 molecule of 'FA anion:UCP dimer "head-out" complex' is present. At the end of this reaction, 1 molecule of 'UCP dimer', and 1 molecule of 'Fatty Acid anion "head-out"' are present.

This reaction takes place in the 'mitochondrial inner membrane'.

REACT_6300 (Reactome) The Protonmotive Q cycle is the mechanism by which complex III transfers electrons from ubiquinol to cytochrome c, linking this process to translocation of protons across the membrane. This cycle is complicated by the fact that both ubiquinol is oxidised and ubiquinone is reduced during this process. Through a complex series of electron transfers, Complex III consumes two molecules of ubiquinol (QH2) and two molecules of oxidized cytochrome c, generates one molecule of ubiquinone (Q) and two molecules of reduced cytochrome c, regenerates one molecule of ubiquinol (QH2), and mediates the translocation of two protons from the mitochondrial matrix to the mitochondrial intermembrane space.

The overall reaction can be summed up as below:
2QH2 + 2cyt c(ox.) + Q + 2H+matrix -> 2Q + 2cyt c(red.) + QH2 + 4H+memb. space



REACT_6302 (Reactome) At the beginning of this reaction, 1 molecule of 'Fatty Acid "head-in"' is present. At the end of this reaction, 1 molecule of 'H+', and 1 molecule of 'Fatty Acid anion "head-in"' are present.

This reaction takes place in the 'mitochondrial inner membrane'.

REACT_6310 (Reactome) Complex I (NADH:ubiquinone oxidoreductase or NADH dehydrogenase) utilizes NADH formed from glycolysis and the TCA cycle to pump protons out of the mitochondrial matrix. It is the largest enzyme complex in the electron transport chain, containing 45 subunits. Seven subunits (ND1-6, ND4L) are encoded by mitochondrial DNA (Loeffen et al [1998]), the remainder are encoded in the nucleus. The enzyme has a FMN prosthetic group and 8 Iron-Sulfur (Fe-S) clusters. The electrons from NADH oxidation pass through the flavin (FMN) and Fe-S clusters to ubiquinone (CoQ). This electron transfer is coupled with the translocation of protons from the mitochondrial matrix to the intermembrane space. For each electron transferred, 2 protons can be pumped out of the matrix. As there are 2 electrons transferred, 4 protons can be pumped out.
Complex I is made up of 3 sub-complexes - Iron-Sulfur protein fraction (IP), Flavoprotein fraction (FP) and the Hydrophobic protein fraction (HP), probably arranged in an L-shaped structure with the IP and FP fractions protruding into the mitochondrial matrix and the HP arm lying within the inner mitochondrial membrane. The overall reaction can be summed as below:
NADH + Ubiquinone + 5H+matrix -> NAD+ + Ubiquinol + 4H+memb. space

The electrons from complex I are transferred to ubiquinone (Coenzyme Q, CoQ), a small mobile carrier of electrons located within the inner membrane. Ubiquinone is reduced to ubiquinol during this process.
REACT_6312 (Reactome) In this reaction, 1 molecule of 'H+' is translocated from mitochondrial intermembrane space to mitochondrial matrix.

This reaction takes place in the 'mitochondrial inner membrane' and is mediated by the 'hydrogen ion transporter activity' of 'UCP dimer'.
REACT_6360 (Reactome) This event is deduced on the basis of bovine experimental data.
Complex II (succinate dehydrogenase) transfers electrons from the TCA cycle to ubiquinone. The 6th step in the TCA cycle is where succinate is dehydrogenated to fumarate with subsequent reduction of FAD to FADH2. FADH2 provides the electrons for the transport chain. Succinate dehydrogenase belongs to subclass 1 of the SQR family (succinate:quinone reductase) (classified by Hagerhall, C and Hederstedt, L [1996]).
It consists of 4 subunits (referred to as A, B, C and D), all nuclear-encoded and is located on the matrix side of the inner mitochondrial membrane. Subunits A and B are hydrophilic whereas subunits C and D are integral proteins of the inner membrane. SQRs usually contain 3 Fe-S clusters bound by the B subunit. Succinate dehydrogenase contains one [2Fe-2S] cluster, one [4Fe-4S] cluster and one [3Fe-4S] cluster. Additionally, the A subunit has a covalently-bound FAD group. Reduced complex II has this FAD converted to FADH2. The electrons from complex II are transferred to ubiquinone (also called Q, Coenzyme Q or CoQ), a small mobile carrier of electrons located within the inner membrane. Ubiquinone is reduced to ubiquinol during this process.
REACT_991 (Reactome) The beta subunit has 3 conformations; tight, open and loose. ADP and Pi bind to the subunit in the loose form. On binding, this subunit is converted to the tight configuration.
Succinate dehydrogenase complex ArrowREACT_6360 (Reactome)
Succinate dehydrogenase complex REACT_6360 (Reactome)
UCP dimerArrowREACT_6218 (Reactome)
UCP dimerREACT_6165 (Reactome)
UCP dimerREACT_6312 (Reactome)
Ubiquinol-cytochrome c reductaseREACT_6300 (Reactome)
Personal tools