Cryo-EM structure of cytochrome bo3 quinol oxidase assembled in peptidiscs reveals an “open” conformation for potential ubiquinone-8 release
Author:
Funder
Health~Holland
Maastricht University
NWO
Publisher
Elsevier BV
Reference39 articles.
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2. Modified, large-scale purification of the cytochrome o complex (Bo-type oxidase) of Escherichia coli yields a two heme/one copper terminal oxidase with high specific activity;Minghetti;Biochemistry,1992
3. Assignment and functional roles of the cyoABCDE gene products required for the Escherichia coli bo-type quinol oxidase;Nakamura;J. Biochem.,1997
4. The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site;Abramson;Nat. Struct. Biol.,2000
5. A ‘Build and Retrieve’ methodology to simultaneously solve cryo-EM structures of membrane proteins;Su;Nat. Methods,2021
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