M
Martin Engelhard
Researcher at Max Planck Society
Publications - 178
Citations - 7704
Martin Engelhard is an academic researcher from Max Planck Society. The author has contributed to research in topics: Sensory rhodopsin II & Bacteriorhodopsin. The author has an hindex of 47, co-authored 175 publications receiving 7372 citations.
Papers
More filters
Journal ArticleDOI
Molecular basis of transmembrane signalling by sensory rhodopsin II–transducer complex
Valentin Gordeliy,Jörg Labahn,Rouslan Moukhametzianov,Rouslan G. Efremov,Joachim Granzin,Ramona Schlesinger,Georg Büldt,Tudor Savopol,Axel J. Scheidig,Johann P. Klare,Martin Engelhard +10 more
TL;DR: The X-ray structure of the complex between N. pharaonis SRII and the receptor-binding domain of HtrII at 1.94 Å resolution provides an atomic picture of the first signal transduction step, providing evidence for a common mechanism for this process in phototaxis and chemotaxis.
Journal ArticleDOI
A new synthetic route to tert-butyloxycarbonylaminoacyl-4-(oxymethyl)phenylacetamidomethyl-resin, an improved support for solid-phase peptide synthesis
Journal ArticleDOI
Bioenergetics of the Archaea
TL;DR: From aerobically respiring archaea, unusual electron-transporting supercomplexes could be isolated and functionally resolved, and a proposal on the organization of archaeal electron transport chains has been presented.
Journal ArticleDOI
Light-driven protonation changes of internal aspartic acids of bacteriorhodopsin: an investigation of static and time-resolved infrared difference spectroscopy using [4-13C]aspartic acid labeled purple membrane
TL;DR: Comparing the difference spectra in the region of the CO2- stretching vibrations of labeled and unlabeled BR indicates that ionized aspartic acids are influenced during the photocycle, the earliest effect being observed already at the K610 intermediate.
Journal ArticleDOI
Proteorhodopsin is a light-driven proton pump with variable vectoriality.
Thomas Friedrich,Sven Geibel,Rolf Kalmbach,Igor Chizhov,Kenichi Ataka,Joachim Heberle,Martin Engelhard,Ernst Bamberg +7 more
TL;DR: The results show that proteorhodopsin is a light-driven proton pump with characteristics similar to those of BR at alkaline pH, however, at acidic pH, the direction of proton pumping is inverted.