Nature Communications (Nov 2019)

Homologous bd oxidases share the same architecture but differ in mechanism

  • Alexander Theßeling,
  • Tim Rasmussen,
  • Sabrina Burschel,
  • Daniel Wohlwend,
  • Jan Kägi,
  • Rolf Müller,
  • Bettina Böttcher,
  • Thorsten Friedrich

DOI
https://doi.org/10.1038/s41467-019-13122-4
Journal volume & issue
Vol. 10, no. 1
pp. 1 – 7

Abstract

Read online

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.