Cryo-EM structure of the four-subunit Rhodobacter sphaeroides cytochrome bc₁ complex in styrene maleic acid nanodiscs.

ABSTRACT: Cytochrome bc₁ complexes are ubiquinol:cytochrome c oxidoreductases, and as such, they are centrally important components of respiratory and photosynthetic electron transfer chains in many species of bacteria and in mitochondria. The minimal complex has three catalytic components, which are cytochrome b, cytochrome c₁, and the Rieske iron-sulfur subunit, but the function of mitochondrial cytochrome bc₁ complexes is modified by up to eight supernumerary subunits. The cytochrome bc₁ complex from the purple phototrophic bacterium Rhodobacter sphaeroides has a single supernumerary subunit called subunit IV, which is absent from current structures of the complex. In this work we use the styrene-m

SUBMITTER: Swainsbury DJK 

PROVIDER: S-EPMC10041115 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature