Structure of a bd oxidase indicates similar mechanisms for membrane-integrated oxygen reductases

Author:

Safarian Schara1,Rajendran Chitra12,Müller Hannelore1,Preu Julia1,Langer Julian D.13,Ovchinnikov Sergey4,Hirose Taichiro5,Kusumoto Tomoichirou5,Sakamoto Junshi5,Michel Hartmut1

Affiliation:

1. Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max-von-Laue-Straße 3, D-60438 Frankfurt/Main, Germany.

2. Present address: Faculty of Biology and Preclinical Medicine, University of Regensburg, Universitätsstrasse 31, D-93051 Regensburg, Germany.

3. Present address: Department of Molecular Membrane Biology, Max Planck Institute for Brain Research, Max-von-Laue-Straße 4, D-60438 Frankfurt/Main, Germany.

4. Department of Biochemistry, University of Washington, Seattle, WA, USA.

5. Department of Bioscience and Bioinformatics, Kyushu Institute of Technology, Kawazu 680-4, Iizuka, Fukuoka-ken 820-8502, Japan.

Abstract

Peering into a membrance oxidase Microorganisms have evolved a number of enzymes to reduce oxygen and prevent oxidative stress. Cytochrome bd oxidases serve this role and also protect pathogenic bacteria from nitric acid; however, this class of enzymes so far has eluded high-resolution crystallography. Safarian et al. were able to resolve the three-dimensional structure of cytochrome bd oxidase from a thermophilic bacterium (see the Perspective by Cook and Poole). The overall structure and triangular arrangement of its heme cofactors bear little structural resemblance to those of other membrane-spanning oxidases, despite serving a similar function. Science , this issue p. 583 ; see also p. 518

Funder

Max Planck Society

Deutsche Forschungsgemeinschaft

Grant-in-Aid for Scientific Research

Japan Society for the Promotion of Science

National Institutes of Health

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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