1qle

From Proteopedia

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 CU, CA, MN, HEA, CUA and PC1 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 Structure known Active Sites: CA, CUA, CUB, HM3, HMA and MM. 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

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