1QLE

CRYO-STRUCTURE OF THE PARACOCCUS DENITRIFICANS FOUR-SUBUNIT CYTOCHROME C OXIDASE IN THE COMPLETELY OXIDIZED STATE COMPLEXED WITH AN ANTIBODY FV FRAGMENT

Summary for 1QLE

• Entry DOI: 10.2210/pdb1qle/pdb
• Related: 1AR1
• Descriptor: CYTOCHROME C OXIDASE POLYPEPTIDE I-BETA, MANGANESE (II) ION, DINUCLEAR COPPER ION, ... (12 entities in total)
• Functional Keywords: oxidoreductase/immune system, complex (oxidoreductase-antibody), electron transport, transmembrane, cytochrome oxidase, antibody complex, oxidoreductase-immune system complex
• Biological source: MUS MUSCULUS (MOUSE); More
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P98002 P08306 P06030; Cell inner membrane; Single-pass membrane protein: P77921
• Total number of polymer chains: 6
• Total formula weight: 152419.56

Authors

Harrenga, A.,Michel, H. (deposition date: 1999-08-30, release date: 1999-12-02, Last modification date: 2024-10-23)

Primary citation

Harrenga, A.,Michel, H.
The Cytochrome C Oxidase from Paracoccus Denitrificans Does not Change the Metal Center Ligation Upon Reduction
J.Biol.Chem., 274:33296-, 1999

PubMed Abstract: 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.

PubMed: 10559205
DOI: 10.1074/JBC.274.47.33296

Experimental method

X-RAY DIFFRACTION (3 Å)