Crystal structure of bacterial cytochrome bc₁ in complex with azoxystrobin reveals a conformational switch of the Rieske iron-sulfur protein subunit.

ABSTRACT: Cytochrome bc₁ complexes (cyt bc₁), also known as complex III in mitochondria, are components of the cellular respiratory chain and of the photosynthetic apparatus of non-oxygenic photosynthetic bacteria. They catalyze electron transfer (ET) from ubiquinol to cytochrome c and concomitantly translocate protons across the membrane, contributing to the cross-membrane potential essential for a myriad of cellular activities. This ET-coupled proton translocation reaction requires a gating mechanism that ensures bifurcated electron flow. Here, we report the observation of the Rieske iron-sulfur protein (ISP) in a mobile state, as revealed by the crystal structure of cyt bc₁ from the photosynthetic bacterium Rhodobacter sphaeroides

SUBMITTER: Esser L 

PROVIDER: S-EPMC6690702 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature