7ose Citations

Structure of Escherichia coli cytochrome bd-II type oxidase with bound aurachin D.

Abstract

Cytochrome bd quinol:O2 oxidoreductases are respiratory terminal oxidases so far only identified in prokaryotes, including several pathogenic bacteria. Escherichia coli contains two bd oxidases of which only the bd-I type is structurally characterized. Here, we report the structure of the Escherichia coli cytochrome bd-II type oxidase with the bound inhibitor aurachin D as obtained by electron cryo-microscopy at 3 Å resolution. The oxidase consists of subunits AppB, C and X that show an architecture similar to that of bd-I. The three heme cofactors are found in AppC, while AppB is stabilized by a structural ubiquinone-8 at the homologous positions. A fourth subunit present in bd-I is lacking in bd-II. Accordingly, heme b595 is exposed to the membrane but heme d embedded within the protein and showing an unexpectedly high redox potential is the catalytically active centre. The structure of the Q-loop is fully resolved, revealing the specific aurachin binding.

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Reviews citing this publication (2)

  1. Bioenergetics and Reactive Nitrogen Species in Bacteria. Borisov VB, Forte E. Int J Mol Sci 23 7321 (2022)
  2. Aurachins, Bacterial Antibiotics Interfering with Electron Transport Processes. Kruth S, Nett M. Antibiotics (Basel) 12 1067 (2023)

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