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Issue 6, 2004
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Sensory rhodopsin II and bacteriorhodopsin: Light activated helix F movement

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Abstract

EPR spectroscopy in combination with site directed spin labeling (SDSL) has become a valuable tool for structural investigations as well as for kinetic studies on proteins. This method has been especially useful for membrane proteins in yielding structural and functional data. This information is not easily available from other techniques, like, e.g., X-ray crystallography or electron microscopy. In the first part of this two part review, the topology of the sensory rhodopsin II/transducer complex (NpSRII/NpHtrII) derived from EPR constraints is compared to that obtained from X-ray crystallography. In the second part, the helix F movement observed for both sensory rhodopsin and bacteriorhodopsin is evaluated and discussed in order to establish a common mechanism after photoreceptor activation.

Graphical abstract: Sensory rhodopsin II and bacteriorhodopsin: Light activated helix F movement

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Article information


Submitted
20 Feb 2004
Accepted
05 Apr 2004
First published
19 May 2004

Photochem. Photobiol. Sci., 2004,3, 543-547
Article type
Perspective

Sensory rhodopsin II and bacteriorhodopsin: Light activated helix F movement

J. P. Klare, E. Bordignon, M. Engelhard and H. Steinhoff, Photochem. Photobiol. Sci., 2004, 3, 543
DOI: 10.1039/B402656J

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