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Biochim Biophys Acta. 2014 May;1837(5):614-25. doi: 10.1016/j.bbabio.2013.09.010. Epub 2013 Sep 20.

Proteorhodopsin.

Author information

1
Max Planck Institute of Biophysics, Max-von-Laue Straße 3, 60438 Frankfurt am Main, Germany. Electronic address: christian.bamann@biophys.mpg.de.
2
Max Planck Institute of Biophysics, Max-von-Laue Straße 3, 60438 Frankfurt am Main, Germany.
3
Johann Wolfgang Goethe University, Institute for Physical and Theoretical Chemistry, Max-von-Laue Straße 7, 60438 Frankfurt am Main, Germany.
4
Johann Wolfgang Goethe University, Institute for Biophysical Chemistry & Centre for Biomolecular Magnetic Resonance, Max-von-Laue Straße 9, 60438 Frankfurt am Main, Germany.

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 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.

KEYWORDS:

Charge transfer; Electrophysiology; NMR spectroscopy; Photocycle; Photoisomerization

PMID:
24060527
DOI:
10.1016/j.bbabio.2013.09.010
[Indexed for MEDLINE]
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