title: Structure of a bd oxidase indicates similar mechanisms for membrane-integrated oxygen reductases.
abstract: The cytochrome bd oxidases are terminal oxidases that are present in bacteria and archaea. They reduce molecular oxygen (dioxygen) to water, avoiding the production of reactive oxygen species. In addition to their contribution to the proton motive force, they mediate viability under oxygen-related stress conditions and confer tolerance to nitric oxide, thus contributing to the virulence of pathogenic bacteria. Here we present the atomic structure of the bd oxidase from Geobacillus thermodenitrificans, revealing a pseudosymmetrical subunit fold. The arrangement and order of the heme cofactors support the conclusions from spectroscopic measurements that the cleavage of the dioxygen bond may be mechanistically similar to that in the heme-copper-containing oxidases, even though the structures are completely different.
authors.affiliation: Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max-von-Laue-Straße 3, D-60438 Frankfurt/Main, Germany.
authors.forename: Schara
authors.initials: S
authors.lastname: Safarian
authors.affiliation: Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max-von-Laue-Straße 3, D-60438 Frankfurt/Main, Germany. Present address: Faculty of Biology and Preclinical Medicine, University of Regensburg, Universitätsstrasse 31, D-93051 Regensburg, Germany.
authors.forename: Chitra
authors.initials: C
authors.lastname: Rajendran
authors.affiliation: Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max-von-Laue-Straße 3, D-60438 Frankfurt/Main, Germany.
authors.forename: Hannelore
authors.initials: H
authors.lastname: Müller
authors.affiliation: Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max-von-Laue-Straße 3, D-60438 Frankfurt/Main, Germany.
authors.forename: Julia
authors.initials: J
authors.lastname: Preu
authors.affiliation: Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max-von-Laue-Straße 3, D-60438 Frankfurt/Main, Germany. Present address: Department of Molecular Membrane Biology, Max Planck Institute for Brain Research, Max-von-Laue-Straße 4, D-60438 Frankfurt/Main, Germany.
authors.forename: Julian D
authors.initials: JD
authors.lastname: Langer
authors.affiliation: Department of Biochemistry, University of Washington, Seattle, WA, USA.
authors.forename: Sergey
authors.initials: S
authors.lastname: Ovchinnikov
authors.affiliation: Department of Bioscience and Bioinformatics, Kyushu Institute of Technology, Kawazu 680-4, Iizuka, Fukuoka-ken 820-8502, Japan.
authors.forename: Taichiro
authors.initials: T
authors.lastname: Hirose
authors.affiliation: Department of Bioscience and Bioinformatics, Kyushu Institute of Technology, Kawazu 680-4, Iizuka, Fukuoka-ken 820-8502, Japan.
authors.forename: Tomoichirou
authors.initials: T
authors.lastname: Kusumoto
authors.affiliation: Department of Bioscience and Bioinformatics, Kyushu Institute of Technology, Kawazu 680-4, Iizuka, Fukuoka-ken 820-8502, Japan.
authors.forename: Junshi
authors.initials: J
authors.lastname: Sakamoto
authors.affiliation: Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max-von-Laue-Straße 3, D-60438 Frankfurt/Main, Germany. hartmut.michel@biophys.mpg.de.
authors.forename: Hartmut
authors.initials: H
authors.lastname: Michel
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000648:ultrastructure; D017937:Cytochrome d Group / Q000737:chemistry* / Q000648:ultrastructure; D045303:Cytochromes b / Q000737:chemistry* / Q000648:ultrastructure; D003576:Electron Transport Complex IV / Q000737:chemistry* / Q000648:ultrastructure; D056506:Geobacillus / Q000201:enzymology*; D010100:Oxygen / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary
chemical_list: D001426:Bacterial Proteins; D017937:Cytochrome d Group; D045303:Cytochromes b; D003576:Electron Transport Complex IV; D010100:Oxygen