Proteorhodopsin.
| Autor: | Bamann C; Max Planck Institute of Biophysics, Max-von-Laue Straße 3, 60438 Frankfurt am Main, Germany. Electronic address: christian.bamann@biophys.mpg.de., Bamberg E; Max Planck Institute of Biophysics, Max-von-Laue Straße 3, 60438 Frankfurt am Main, Germany., Wachtveitl J; Johann Wolfgang Goethe University, Institute for Physical and Theoretical Chemistry, Max-von-Laue Straße 7, 60438 Frankfurt am Main, Germany., Glaubitz C; Johann Wolfgang Goethe University, Institute for Biophysical Chemistry & Centre for Biomolecular Magnetic Resonance, Max-von-Laue Straße 9, 60438 Frankfurt am Main, Germany. |
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| Jazyk: | angličtina |
| Zdroj: | Biochimica et biophysica acta [Biochim Biophys Acta] 2014 May; Vol. 1837 (5), pp. 614-25. Date of Electronic Publication: 2013 Sep 20. |
| DOI: | 10.1016/j.bbabio.2013.09.010 |
| Abstrakt: | 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 particular mode 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. (© 2013 Elsevier B.V. All rights reserved.) |
| Databáze: | MEDLINE |
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