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Proteorhodopsin

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Bamann,  Christian
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137592

Bamberg,  Ernst
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Bamann, C., Bamberg, E., Wachtveitl, J., & Glaubitz, C. (2014). Proteorhodopsin. Biochimica et Biophysica Acta, Bioenergetics, 1837(5), 614-625. doi:10.1016/j.bbabio.2013.09.010.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-D454-3
Abstract
Proteorhodopsins are the most abundant retinal based photoreceptors and their phototrophic function might be relevant in marine ecosystems. Here, we describe their remarkable molecular properties with a special focus on the green absorbing variant. Its distinct features include a high pKa value of the primary proton acceptor stabilized through an interaction with a conserved histidine, a long-range interaction between the cytoplasmic EF loop and the chromophore entailing a particularmode of color tuning and a variable proton pumping vectoriality with complex voltage-dependence. The proteorhodopsin family represents a profound example for structure–function relationships. Especially the development of a biophysical understanding of green proteorhodopsin is an excellent example for the unique opportunities offered by a combined approach of advanced spectroscopic and electrophysiological methods. This article is part of a Special Issue entitled: Retinal Proteins—You can teach an old dog new tricks.