C
Christian Bamann
Researcher at Max Planck Society
Publications - 47
Citations - 2896
Christian Bamann is an academic researcher from Max Planck Society. The author has contributed to research in topics: Bacteriorhodopsin & Rhodopsin. The author has an hindex of 27, co-authored 46 publications receiving 2591 citations. Previous affiliations of Christian Bamann include Commissariat à l'énergie atomique et aux énergies alternatives.
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Journal ArticleDOI
Ultra light-sensitive and fast neuronal activation with the Ca2+-permeable channelrhodopsin CatCh
Sonja Kleinlogel,Katrin Feldbauer,Robert E. Dempski,Heike Fotis,Phillip G. Wood,Christian Bamann,Ernst Bamberg +6 more
TL;DR: A new variant, calcium translocating channelrhodopsin (CatCh), is presented, which mediates an accelerated response time and a voltage response that is ∼70-fold more light sensitive than that of wild-type ChR2 and paves the way for clinical use of light-gated channels.
Journal ArticleDOI
Spectral Characteristics of the Photocycle of Channelrhodopsin-2 and Its Implication for Channel Function
TL;DR: It is concluded that the red-shifted spectral species represents the open channel state, and the thermal relaxation of this intermediate, the transition from P(3) to P(4), is coupled to channel closing.
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Structural Guidance of the Photocycle of Channelrhodopsin-2 by an Interhelical Hydrogen Bond
TL;DR: Slow mutants of ChR2 generated by disturbing a postulated hydrogen bond when mutating C128 in the transmembrane (TM) helix 3 and D156 in TM helix 4 conclude that the putative hydrogen bond between C128 and D 156 is an important structural determinant of the channel's closing reaction.
Journal ArticleDOI
Channelrhodopsin-2 is a leaky proton pump
Katrin Feldbauer,Dirk Zimmermann,Verena Pintschovius,Julia Spitz,Christian Bamann,Ernst Bamberg +5 more
TL;DR: It is shown that when ChR2 is expressed in electrofused giant HEK293 cells or reconstituted on planar lipid membranes, it can indeed act as an outwardly driven H+ pump, demonstrating that ChR 2 is bifunctional, and in-line with other microbial rhodopsins, a H+ Pump but with a leak that shows ion channel properties.
Journal ArticleDOI
Transient protonation changes in channelrhodopsin-2 and their relevance to channel gating
Víctor A. Lórenz-Fonfría,Tom Resler,Nils Krause,Melanie Nack,Michael Gossing,Gabriele Fischer von Mollard,Christian Bamann,Ernst Bamberg,Ramona Schlesinger,Joachim Heberle +9 more
TL;DR: The structural changes of ChR2 are traced by time-resolved FTIR spectroscopy, complemented by functional electrophysiological measurements and a mechanistic proposal relates the observed proton transfer reactions and the protein conformational changes to the gating of the cation channel.