1qle
From Proteopedia
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | Cytochrome c oxidase catalyzes the reduction of oxygen to water. This | + | 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. |
==About this Structure== | ==About this Structure== | ||
| Line 30: | Line 30: | ||
[[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:40:56 2008'' |
Revision as of 12:41, 21 February 2008
|
CRYO-STRUCTURE OF THE PARACOCCUS DENITRIFICANS FOUR-SUBUNIT CYTOCHROME C OXIDASE IN THE COMPLETELY OXIDIZED STATE COMPLEXED WITH AN ANTIBODY FV FRAGMENT
Overview
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.
About this Structure
1QLE is a Protein complex structure of sequences from Mus musculus and Paracoccus denitrificans with , , , , and as ligands. The following page contains interesting information on the relation of 1QLE with [Cytochrome c Oxidase]. Active as Cytochrome-c oxidase, with EC number 1.9.3.1 Known structural/functional Sites: , , , , and . Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 14:40:56 2008
