Eva Schäfer

TL;DR: In this paper, electron microscopic characterization of the two respiratory chain supercomplexes I1III2 and I 1III2IV1 in bovine heart mitochondria, which are also two major super-complexes in human mitochondria.

TL;DR: Observations in mitochondria show that the mitochondrial inner membrane is highly organised and that the molecular events leading to ATP synthesis are carefully coordinated.

TL;DR: The first 3D map of a respiratory chain supercomplex was determined by random conical tilt electron microscopy analysis of a bovine supercomplex consisting of complex I, dimeric complex III, and complex IV and provided structural evidence for direct substrate channeling in the supercomplex assembly with short diffusion distances for the mobile electron carriers.

TL;DR: A variety of aspects of energy-transducing membranes from large protein complexes down to the level of protons and functional relevant picosecond protein dynamics are examined, based on the central role of the ATP synthase for supplying the biological fuel ATP.

TL;DR: It is shown that the reactivity of the ATP synthase alpha subunit is not randomly distributed over the ATP Synthase, but is channeled to a single tryptophan residue 503, which serves as an intra-molecular quencher for oxidative species and might also be involved in the metabolic perception of oxidative stress or regulation of enzyme activity.