Journal
SCIENCE
Volume 352, Issue 6285, Pages 583-586Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aaf2477
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Funding
- Max Planck Society
- Japan Society for the Promotion of Science [25440050]
- National Institutes of Health [R01GM092802]
- Deutsche Forschungsgemeinschaft (Cluster of Excellence Macromolecular Complexes Frankfurt)
- Grants-in-Aid for Scientific Research [25440050] Funding Source: KAKEN
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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.
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