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- Title
Structure and mechanism of the aberrant ba<sub>3</sub>-cytochrome c oxidase from Thermus thermophilus.
- Authors
Soulimane, Tewfik; Buse, Gerhard; Bourenkov, Gleb P.; Bartunik, Hans D.; Huber, Robert; Than, Manuel E.
- Abstract
Cytochrome c oxidase is a respiratory enzyme catalysing the energy-conserving reduction of molecular oxygen to water. The crystal structure of the ba3 cytochrome c oxidase from Thermus thermophilus has been determined to 2.4 Å resolution using multiple anomalous dispersion (MAD) phasing and led to the discovery of a novel subunit IIa. A structure-based sequence alignment of this phylogenetically very distant oxidase with the other structurally known cytochrome oxidases leads to the identification of sequence motifs and residues that seem to be indispensable for the function of the haem copper oxidases, e.g. a new electron transfer pathway leading directly from CUA to CUB. Specific features of the ba3-oxidase include an extended oxygen input channel, which leads directly to the active site, the presence of only one oxygen atom (02-, OH- or H2O) as bridging ligand at the active site and the mainly hydrophobic character of the interactions that stabilize the electron transfer complex between this oxidase and its substrate cytochrome c. New aspects of the proton pumping mechanism could be identified.
- Subjects
PROKARYOTES; CYTOCHROME oxidase; MICROBIAL enzymes; MEMBRANE proteins; CHEMICAL reduction; PHYLOGENY; HOMOLOGY (Biology)
- Publication
EMBO Journal, 2000, Vol 19, Issue 8, p1766
- ISSN
0261-4189
- Publication type
Article
- DOI
10.1093/emboj/19.8.1766