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| Title | Homologous bd oxidases share the same architecture but differ in mechanism. |
|---|---|
| Journal, issue, pages | Nat Commun, Vol. 10, Issue 1, Page 5138, Year 2019 |
| Publish date | Nov 13, 2019 |
 Authors | Alexander Theßeling / Tim Rasmussen / Sabrina Burschel / Daniel Wohlwend / Jan Kägi / Rolf Müller / Bettina Böttcher / Thorsten Friedrich /  |
| PubMed Abstract | 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 ...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 b 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. |
 External links | Nat Commun / PubMed:31723136 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.3 Å |
| Structure data | EMDB-10049, PDB-6rx4: |
| Chemicals |  ChemComp-HEB:  ChemComp-HDD:  ChemComp-PEE:  ChemComp-UQ8:  ChemComp-HOH: |
| Source |
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 Keywords |  OXIDOREDUCTASE / BD OXIDASE / TERMINAL OXIDASE |
