Safarian, Schara and Rajendran, Chitra and Mueller, Hannelore and Preu, Julia and Langer, Julian D. and Ovchinnikov, Sergey and Hirose, Taichiro and Kusumoto, Tomoichirou and Sakamoto, Junshi and Michel, Hartmut (2016) Structure of a bd oxidase indicates similar mechanisms for membrane-integrated oxygen reductases. SCIENCE, 352 (6285). pp. 583-586. ISSN 0036-8075, 1095-9203
Full text not available from this repository. (Request a copy)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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | RADICAL CATALYTIC INTERMEDIATE; SITE-DIRECTED MUTAGENESIS; AEROBIC RESPIRATORY-CHAIN; CYTOCHROME-C-OXIDASE; HEME ACTIVE-SITE; ESCHERICHIA-COLI; QUINOL OXIDASE; AZOTOBACTER-VINELANDII; TERMINAL OXIDASES; BINUCLEAR CENTER; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 21 Mar 2019 09:42 |
| Last Modified: | 21 Mar 2019 09:42 |
| URI: | https://pred.uni-regensburg.de/id/eprint/3053 |
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