ArticleNature communications2019
Homologous bd oxidases share the same architecture but differ in mechanism.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 94 citations in OpenAlex.
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- Preventive treatment of tripdiolide ameliorates kidney injury in diabetic mice by modulating the Nrf2/NF-κB pathway.Frontiers in pharmacology · 2025Article
- Modifications of the respiratory chain of Bacillus licheniformis as an alkalophilic and cyanide-degrading microorganism.Journal of bioenergetics and biomembranes · 2024Article
- Large Roles of Small Proteins.Annual review of microbiology · 2024Review
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- CytochromeRSC medicinal chemistry · 2024Review
- Membrane-Bound Redox Enzyme CytochromeInternational journal of molecular sciences · 2024Article
- Editorial: Computational and experimental insights in proton and ion translocating bioenergetic systems.Frontiers in chemistry · 2024Article
- MSTL-Kace: Prediction of Prokaryotic Lysine Acetylation Sites Based on Multistage Transfer Learning Strategy.ACS omega · 2023Article
- Dissecting the conformational complexity and mechanism of a bacterial heme transporter.Nature chemical biology · 2023Article
- Exploring ND-011992, a quinazoline-type inhibitor targeting quinone reductases and quinol oxidases.Scientific reports · 2023Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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 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
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