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Active site rearrangement and structural divergence in prokaryotic respiratory oxidases.

08:00 EDT 4th October 2019 | BioPortfolio

Summary of "Active site rearrangement and structural divergence in prokaryotic respiratory oxidases."

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 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.

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This article was published in the following journal.

Name: Science (New York, N.Y.)
ISSN: 1095-9203
Pages: 100-104

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Medical and Biotech [MESH] Definitions

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