Homologous bd oxidases share the same architecture but differ in mechanism.
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Authors
Theßeling, AlexanderRasmussen, Tim
Burschel, Sabrina
Wohlwend, Daniel
Kägi, Jan
Müller, Rolf
Böttcher, Bettina
Friedrich, Thorsten
Issue Date
2019-11-13
Metadata
Show full item recordAbstract
Cytochrome bd oxidases are terminal reductases of bacterial and archaeal respiratory chains. The enzyme couples the oxidation of ubiquinol or menaquinol with the reduction of dioxygen to water, thus contributing to the generation of the protonmotive force. Here, we determine the structure of the Escherichia coli bd oxidase treated with the specific inhibitor aurachin by cryo-electron microscopy (cryo-EM). The major subunits CydA and CydB are related by a pseudo two fold symmetry. The heme b and d cofactors are found in CydA, while ubiquinone-8 is bound at the homologous positions in CydB to stabilize its structure. The architecture of the E. coli enzyme is highly similar to that of Geobacillus thermodenitrificans, however, the positions of heme b595 and d are interchanged, and a common oxygen channel is blocked by a fourth subunit and substituted by a more narrow, alternative channel. Thus, with the same overall fold, the homologous enzymes exhibit a different mechanism.Citation
Nat Commun. 2019 Nov 13;10(1):5138. doi: 10.1038/s41467-019-13122-4.Affiliation
HIPS, Helmholtz-Institut für Pharmazeutische Forschung Saarland, Universitätscampus E8.1 66123 Saarbrücken, Germany.Publisher
Nature Publication groupJournal
Nature communicationsPubMed ID
31723136Type
ArticleLanguage
enISSN
2041-1723ae974a485f413a2113503eed53cd6c53
10.1038/s41467-019-13122-4
Scopus Count
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- Creative Commons
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