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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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Publication details

The article was received on 20 Feb 2004, accepted on 05 Apr 2004 and first published on 19 May 2004


Article type: Perspective
DOI: 10.1039/B402656J
Citation: Photochem. Photobiol. Sci., 2004,3, 543-547

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    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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