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Showing 1–3 of 3 results
Advanced filters: Author: Sabrina Burschel Clear advanced filters

  • Cytochrome bd oxidases couple quinol oxidation and the release of protons to the periplasmic side with proton uptake from the cytoplasmic side to reduce dioxygen to water and they are the terminal reductases in bacterial and archaeal respiratory chains. Here the authors present the cryo-EM structure of Escherichia coli bd oxidase and discuss mechanistic implications.

    • Alexander Theßeling
    • Tim Rasmussen
    • Thorsten Friedrich
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-7

  • Respiratory complex I plays a central role in cellular energy metabolism coupling NADH oxidation to proton translocation. Here, the authors report the structure of the electron input part of Aquifex aeolicus complex I at up to 1.8 Å resolution with bound substrates in the reduced and oxidized states.

    • Marius Schulte
    • Klaudia Frick
    • Thorsten Friedrich
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-9

  • Antibiotic persisters are phenotypic variants within an isogenic bacterial population that are transiently tolerant to antibiotic treatment. Here, the authors provide evidence that cytoplasmic acidification, amplified by a compromised respiratory complex I, can act as a signaling hub for perturbed metabolic homeostasis in antibiotic persisters.

    • Bram Van den Bergh
    • Hannah Schramke
    • Matthias Heinemann
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-18