Structural highlights
1qle is a 6 chain structure with sequence from Lk3 transgenic mice and Paracoccus denitrificans. The May 2000 RCSB PDB Molecule of the Month feature on Cytochrome c Oxidase by David S. Goodsell is 10.2210/rcsb_pdb/mom_2000_5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , , , |
| Related: | 1ar1 |
| Activity: | Cytochrome-c oxidase, with EC number 1.9.3.1 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum |
Function
[COX4_PARDE] Not required for enzymatic activity or proton pumping of the cytochrome c oxidase complex.[1] [COX1B_PARDE] Subunit I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. [COX2_PARDE] Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Cytochrome c oxidase catalyzes the reduction of oxygen to water. This process is accompanied by the vectorial transport of protons across the mitochondrial or bacterial membrane ("proton pumping"). The mechanism of proton pumping is still a matter of debate. Many proposed mechanisms require structural changes during the reaction cycle of cytochrome c oxidase. Therefore, the structure of the cytochrome c oxidase was determined in the completely oxidized and in the completely reduced states at a temperature of 100 K. No ligand exchanges or other major structural changes upon reduction of the cytochrome c oxidase from Paracoccus denitrificans were observed. The three histidine Cu(B) ligands are well defined in the oxidized and in the reduced states. These results are hardly compatible with the "histidine cycle" mechanisms formulated previously.
The cytochrome c oxidase from Paracoccus denitrificans does not change the metal center ligation upon reduction.,Harrenga A, Michel H J Biol Chem. 1999 Nov 19;274(47):33296-9. PMID:10559205[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Witt H, Ludwig B. Isolation, analysis, and deletion of the gene coding for subunit IV of cytochrome c oxidase in Paracoccus denitrificans. J Biol Chem. 1997 Feb 28;272(9):5514-7. PMID:9038156
- ↑ Harrenga A, Michel H. The cytochrome c oxidase from Paracoccus denitrificans does not change the metal center ligation upon reduction. J Biol Chem. 1999 Nov 19;274(47):33296-9. PMID:10559205
