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Enzyme Name | UniProtKB | KEGG |
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| Q56408 | Q5SJ79 | P98052 | Q5SJ80 | P82543 |
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Protein name | Cytochrome c oxidase subunit 1 | Cytochrome c oxidase subunit 1 | Cytochrome c oxidase subunit 2 | Cytochrome c oxidase subunit 2 | Cytochrome c oxidase polypeptide 2A | cytochrome-c oxidasecytochrome oxidasecytochrome a3cytochrome aa3Warburg's respiratory enzymeindophenol oxidaseindophenolasecomplex IV (mitochondrial electron transport)ferrocytochrome c oxidaseNADH cytochrome c oxidase |
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Synonyms | EC 1.9.3.1Cytochrome c ba(3) subunit ICytochrome c oxidase polypeptide ICytochrome cba3 subunit 1 | EC 1.9.3.1Cytochrome c ba(3) subunit ICytochrome c oxidase polypeptide ICytochrome cba3 subunit 1 | EC 1.9.3.1Cytochrome c ba(3) subunit IICytochrome c oxidase polypeptide IICytochrome cba3 subunit 2 | EC 1.9.3.1Cytochrome c ba(3) subunit IICytochrome c oxidase polypeptide IICytochrome cba3 subunit 2 | EC 1.9.3.1Cytochrome c ba(3) subunit IIACytochrome c oxidase polypeptide IIACytochrome cba3 subunit 2A |
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RefSeq |
| YP_144401.1 (Protein) NC_006461.1 (DNA/RNA sequence)
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| YP_144400.1 (Protein) NC_006461.1 (DNA/RNA sequence)
| YP_144399.1 (Protein) NC_006461.1 (DNA/RNA sequence)
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Pfam | PF00115 (COX1) [Graphical view]
| PF00115 (COX1) [Graphical view]
| PF00116 (COX2) [Graphical view]
| PF00116 (COX2) PF09125 (COX2-transmemb) [Graphical view]
| PF08113 (CoxIIa) [Graphical view]
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KEGG pathways | MAP code | Pathways |
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MAP00190 | Oxidative phosphorylation |
UniProtKB:Accession Number | Q56408 | Q5SJ79 | P98052 | Q5SJ80 | P82543 |
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Entry name | COX1_THETH | COX1_THET8 | COX2_THETH | COX2_THET8 | COXA_THET8 |
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Activity | 4 ferrocytochrome c + O(2) + 4 H(+) = 4 ferricytochrome c + 2 H(2)O. | 4 ferrocytochrome c + O(2) + 4 H(+) = 4 ferricytochrome c + 2 H(2)O. | 4 ferrocytochrome c + O(2) + 4 H(+) = 4 ferricytochrome c + 2 H(2)O. | 4 ferrocytochrome c + O(2) + 4 H(+) = 4 ferricytochrome c + 2 H(2)O. | 4 ferrocytochrome c + O(2) + 4 H(+) = 4 ferricytochrome c + 2 H(2)O. |
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Subunit |
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Subcellular location | Cell membrane, Multi-pass membrane protein (By similarity). | Cell membrane, Multi-pass membrane protein. | Cell membrane, Peripheral membrane protein. | Cell membrane, Single-pass membrane protein. | Cell membrane, Single-pass membrane protein. |
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Cofactor | Binds 2 heme groups (By similarity).,Copper B (By similarity). | Binds 2 heme groups (By similarity).,Copper B (By similarity). |
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Compound table: links to PDB-related databases & PoSSuM |
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| Cofactors | Substrates | Products |
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KEGG-id | C00070 | C00032 | C00032 | C00126 | C00007 | C00125 | C00001 |
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Compound | Copper | Heme A | Heme A3 | Ferrocytochrome c | O2 | Ferricytochrome c | H2O |
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Type | heavy metal | aromatic ring (with nitrogen atoms),carboxyl group,heavy metal | aromatic ring (with nitrogen atoms),carboxyl group,heavy metal | amide group,amine group,aromatic ring (with nitrogen atoms),carboxyl group,heavy metal,sulfide group | others | amide group,amine group,aromatic ring (with nitrogen atoms),carboxyl group,heavy metal,sulfide group | H2O |
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ChEBI | 28694 30052
| 17627 26355
| 17627 26355
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| 15379 26689 27140
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| 15377
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PubChem | 23978
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| 977
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| 22247451 962
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| | | | | | | | | | | | | | |
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1xmeA |  |  |  |  |  |  |  | Bound:_CU | Analogue:HEM | Analogue:HAS | Unbound | Unbound | Unbound | |
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1ehkA |  |  |  |  |  |  |  | Bound:_CU | Analogue:HEM | Analogue:HAS | Unbound | Unbound | Unbound | |
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1xmeB01 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
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1ehkB01 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
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2fwlB01 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
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1xmeB02 |  |  |  |  |  |  |  | Bound:CUA | Unbound | Unbound | Unbound | Unbound | Unbound | |
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1ehkB02 |  |  |  |  |  |  |  | Bound:CUA | Unbound | Unbound | Unbound | Unbound | Unbound | |
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2fwlB02 |  |  |  |  |  |  |  | Bound:CUA | Unbound | Unbound | Bound:HEC(chain A) | Unbound | Unbound | |
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2cuaA |  |  |  |  |  |  |  | Bound:CUA | Unbound | Unbound | Unbound | Unbound | Unbound | |
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2cuaB |  |  |  |  |  |  |  | Bound:CUA | Unbound | Unbound | Unbound | Unbound | Unbound | |
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1xmeC |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
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1ehkC |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[8] | p.1770-1773 |
| [11] | Fig.10, p.14511-14512 |
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references | [1] |
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PubMed ID | 7615066 |
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Journal | FEBS Lett |
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Year | 1995 |
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Volume | 368 |
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Pages | 132-4 |
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Authors | Soulimane T, Gohlke U, Huber R, Buse G |
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Title | Three-dimensional crystals of cytochrome-c oxidase from Thermus thermophilus diffracting to 3.8 A resolution. |
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[2] |
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PubMed ID | 9399580 |
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Journal | J Biochem (Tokyo) |
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Year | 1997 |
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Volume | 122 |
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Pages | 764-71 |
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Authors | Sakamoto J, Handa Y, Sone N |
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Title | A novel cytochrome b(o/a)3-type oxidase from Bacillus stearothermophilus catalyzes cytochrome c-551 oxidation. |
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[3] |
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PubMed ID | 9299406 |
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Journal | Biochem Biophys Res Commun |
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Year | 1997 |
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Volume | 237 |
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Pages | 572-6 |
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Authors | Soulimane T, von Walter M, Hof P, Than ME, Huber R, Buse G |
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Title | Cytochrome-c552 from Thermus thermophilus: a functional and crystallographic investigation. |
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[4] |
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PubMed ID | 9281430 |
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Journal | J Mol Biol |
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Year | 1997 |
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Volume | 271 |
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Pages | 629-44 |
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Authors | Than ME, Hof P, Huber R, Bourenkov GP, Bartunik HD, Buse G, Soulimane T |
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Title | Thermus thermophilus cytochrome-c552: A new highly thermostable cytochrome-c structure obtained by MAD phasing. |
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[5] |
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PubMed ID | 10486572 |
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Journal | FEBS Lett |
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Year | 1999 |
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Volume | 457 |
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Pages | 98-102 |
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Authors | Siletskiy S, Soulimane T, Azarkina N, Vygodina TV, Buse G, Kaulen A, Konstantinov A |
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Title | Time-resolved generation of a membrane potential by ba3 cytochrome c oxidase from Thermus thermophilus. Evidence for reduction-induced opening of the binuclear center. |
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[6] |
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Comments | X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) |
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Medline ID | 99287095 |
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PubMed ID | 10360350 |
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Journal | Nat Struct Biol |
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Year | 1999 |
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Volume | 6 |
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Pages | 509-16 |
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Authors | Williams PA, Blackburn NJ, Sanders D, Bellamy H, Stura EA, Fee JA, McRee DE |
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Title | The CuA domain of Thermus thermophilus ba3-type cytochrome c oxidase at 1.6 A resolution. |
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Related PDB | 2cua |
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Related UniProtKB | P98052 |
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[7] |
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PubMed ID | 11152118 |
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Journal | Protein Sci |
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Year | 2000 |
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Volume | 9 |
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Pages | 2068-73 |
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Authors | Soulimane T, Than ME, Dewor M, Huber R, Buse G |
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Title | Primary structure of a novel subunit in ba3-cytochrome oxidase from Thermus thermophilus. |
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[8] |
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Comments | X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) |
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Medline ID | 20237613 |
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PubMed ID | 10775261 |
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Journal | EMBO J |
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Year | 2000 |
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Volume | 19 |
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Pages | 1766-76 |
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Authors | Soulimane T, Buse G, Bourenkov GP, Bartunik HD, Huber R, Than ME |
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Title | Structure and mechanism of the aberrant ba(3)-cytochrome c oxidase from thermus thermophilus. |
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Related PDB | 1ehk |
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Related UniProtKB | P98052,P82543 |
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[9] |
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PubMed ID | 11716725 |
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Journal | J Am Chem Soc |
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Year | 2001 |
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Volume | 123 |
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Pages | 11678-85 |
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Authors | Fernandez CO, Cricco JA, Slutter CE, Richards JH, Gray HB, Vila AJ |
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Title | Axial ligand modulation of the electronic structures of binuclear copper sites: analysis of paramagnetic 1H NMR spectra of Met160Gln Cu(A). |
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[10] |
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PubMed ID | 15735345 |
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Journal | Acta Crystallogr D Biol Crystallogr |
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Year | 2005 |
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Volume | 61 |
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Pages | 340-3 |
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Authors | Hunsicker-Wang LM, Pacoma RL, Chen Y, Fee JA, Stout CD |
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Title | A novel cryoprotection scheme for enhancing the diffraction of crystals of recombinant cytochrome ba3 oxidase from Thermus thermophilus. |
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Related PDB | 1xme |
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[11] |
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PubMed ID | 16554303 |
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Journal | J Biol Chem |
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Year | 2006 |
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Volume | 281 |
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Pages | 14503-13 |
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Authors | Muresanu L, Pristovsek P, Lohr F, Maneg O, Mukrasch MD, Ruterjans H, Ludwig B, Lucke C |
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Title | The electron transfer complex between cytochrome c552 and the CuA domain of the Thermus thermophilus ba3 oxidase. A combined NMR and computational approach. |
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Related PDB | 2fwl |
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comments | Although this enzyme is partially homologous to that from P. denitrificans (Bacteria) (M00062 in EzCatDB), the subunit/domain compositions seem to be slightly different from the counterpart enzyme. Bacterial enzymes are composed of 3 or 4 subunits. Subunits I and II form the functional core of the enzyme complex. The subunit I binds a copper ion (CuB), two heme groups (heme A and heme A3). The subunit II binds a binuclear copper ion pair, CuA. Heme A3 and CuB form a binuclear centre for O2 reduction. Taken together, this enzyme catalyzes the following reactions, electron transfers and dioxygen reduction, coupling with proton pumping. 4 cyt c(red) + 8 H+(in) + O2 = 4 cyt c(ox) + 2 H2O + 4 H+(out) This enzyme catalyzes the following reactions: (A) Electron transfer from ba3-cytochrome c (substrate;ferrocytochrome c) to CuA (subunit II): (B) Electron transfer from CuA (subunit II) to heme A (subunit I): (C) Electron transfer from heme A (subunit I) to binculear center (heme A3 & CuB) (subunit I): (D) Electron transfer from CuA (subunit II) directly to CuB (subunit I): (E) Reduction of dioxygen (O2) to H2O (at the binuclear center): (F) Proton pump: According to the literature [8] and [11], the following reaction proceeds as follows: (A) Electron transfer from cytochrome c (substrate;ferrocytochrome c) to CuA (subunit II): (A1) Indirect transfer through mainchain atoms of Ala87 and Phe88 (subunit II) to Met160 bound to CuA-1 (see [11]). (B) Electron transfer from CuA (subunit II) to heme A (subunit I): (B1) Indirect transfer through His157 (subunit II), mainchain carbonyl oxygen of Arg449 and mainchain amide of Arg450 (subunit I), and propionate (carboxylate) group of heme A (see M00062). (C) Electron transfer from heme A (subunit I) to binculear center (heme A3 & CuB) (subunit I): (C1) Indirect transfer through His386 bound to heme A iron, mainchain of Phe385, and His384 bound to heme A3 iron (see M00062). On the other hand, the literature [8] proposed an additional electron pathway between CuA (subunit II) and CuB (subunit I). (D) Electron transfer from CuA (subunit II) directly to CuB (subunit I): (D1) Indirect transfer through Gln151 bound to CuA (subunit I), via Tyr136 and Trp229, and His283 bound to CuB (subunit I) (see [8]).
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created | updated |
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2004-03-24 | 2009-02-26 |
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