Long-range charge transfer mechanism of the III₂IV₂ mycobacterial supercomplex.

ABSTRACT: Aerobic life is powered by membrane-bound redox enzymes that shuttle electrons to oxygen and transfer protons across a biological membrane. Structural studies suggest that these energy-transducing enzymes operate as higher-order supercomplexes, but their functional role remains poorly understood and highly debated. Here we resolve the functional dynamics of the 0.7 MDa III₂IV₂ obligate supercomplex from Mycobacterium smegmatis, a close relative of M. tuberculosis, the causative agent of tuberculosis. By combining computational, biochemical, and high-resolution (2.3 Å) cryo-electron microscopy experiments, we show how the mycobacterial supercomplex catalyses long-range charge transport from its menaquinol oxidation site to the binuclear active site for oxygen reduction

SUBMITTER: Riepl D 

PROVIDER: S-EPMC11189923 | biostudies-literature | 2024 Jun

REPOSITORIES: biostudies-literature