title: Structure and mechanism of the aberrant ba(3)-cytochrome c oxidase from thermus thermophilus.
abstract: Cytochrome c oxidase is a respiratory enzyme catalysing the energy-conserving reduction of molecular oxygen to water. The crystal structure of the ba(3)-cytochrome c oxidase from Thermus thermophilus has been determined to 2.4 A 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 Cu(A) to Cu(B). Specific features of the ba(3)-oxidase include an extended oxygen input channel, which leads directly to the active site, the presence of only one oxygen atom (O(2-), OH(-) or H(2)O) 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.
authors.affiliation: Rheinisch-Westfälische Technische Hochschule Aachen, Institut für Biochemie, Pauwelsstrasse 30, D-52057 Aachen, Germany. tsoulimane@post.klinikum.rwth-aachen.de
authors.forename: T
authors.initials: T
authors.lastname: Soulimane
authors.forename: G
authors.initials: G
authors.lastname: Buse
authors.forename: G P
authors.initials: GP
authors.lastname: Bourenkov
authors.forename: H D
authors.initials: HD
authors.lastname: Bartunik
authors.forename: R
authors.initials: R
authors.lastname: Huber
authors.forename: M E
authors.initials: ME
authors.lastname: Than
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D018360:Crystallography, X-Ray; D003573:Cytochrome b Group / Q000737:chemistry* / Q000378:metabolism; D004579:Electron Transport; D003576:Electron Transport Complex IV / Q000737:chemistry* / Q000378:metabolism; D008024:Ligands; D008565:Membrane Proteins / Q000737:chemistry; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010100:Oxygen / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011522:Protons; D017386:Sequence Homology, Amino Acid; D016963:Thermus thermophilus / Q000201:enzymology*
chemical_list: D003573:Cytochrome b Group; D008024:Ligands; D008565:Membrane Proteins; D011522:Protons; C058557:cytochrome ba3; D003576:Electron Transport Complex IV; D010100:Oxygen