Holger Seelert

TL;DR: This work has imaged the ATP synthase from leaf chloroplasts by using atomic force microscopy and, surprisingly, finds that its turbine has 14 subunits, arranged in a cylindrical ring.

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: It is demonstrated for the first time that in green plant tissue a substantial proportion of the respiratory complex IV is assembled with complexes I and III into “respirasome”-like supercomplexes, previously observed in mammalian, fungal, and non-green plant mitochondria only.

TL;DR: Three fundamentally different chloroplast ATP synthase samples of increasing complexity were visualized by atomic force microscopy and a correlation between the presence of subunit IV in the imaged sample and the appearance of a central protrusion in the narrower orifice of the oligomeric cylinder III14 has been observed.

TL;DR: Atomic force microscopy allowed individual subunits of the cylindrical transmembrane rotors from spinach chloroplast and from Ilyobacter tartaricus ATP synthase to be directly visualized in their native‐like environment and suggested the rotor diameter and stoichiometry to be determined by the shape of the subunits and their nearest neighbor interactions.