Active site rearrangement and structural divergence in prokaryotic respiratory oxidases

S. Safarian, A. Hahn, D. J. Mills, M. Radloff, M. L. Eisinger, A. Nikolaev, J. Meier-Credo, F. Melin, H. Miyoshi, R. B. Gennis, J. Sakamoto, J. D. Langer, P. Hellwig, W. Kühlbrandt, H. Michel

Research output: Contribution to journalArticlepeer-review


Cytochrome bd–type quinol oxidases catalyze the reduction of molecular oxygen to water in the respiratory chain of many human-pathogenic bacteria. They are structurally unrelated to mitochondrial cytochrome c oxidases and are therefore a prime target for the development of antimicrobial drugs. We determined the structure of the Escherichia coli cytochrome bd-I oxidase by single-particle cryo–electron microscopy to a resolution of 2.7 angstroms. Our structure contains a previously unknown accessory subunit CydH, the L-subfamily–specific Q-loop domain, a structural ubiquinone-8 cofactor, an active-site density interpreted as dioxygen, distinct water-filled proton channels, and an oxygen-conducting pathway. Comparison with another cytochrome bd oxidase reveals structural divergence in the family, including rearrangement of high-spin hemes and conformational adaption of a transmembrane helix to generate a distinct oxygen-binding site.

Original languageEnglish (US)
Pages (from-to)100-104
Number of pages5
Issue number6461
StatePublished - Oct 4 2019

ASJC Scopus subject areas

  • General


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