Sensory rhodopsin II and bacteriorhodopsin: Light activated helix F movement

Autor(en): Klare, Johann P.
Bordignon, Enrica
Engelhard, Martin
Steinhoff, Heinz-Jurgen 
Stichwörter: Biochemistry & Molecular Biology; Biophysics; Chemistry; Chemistry, Physical; COGNATE TRANSDUCER; CONFORMATIONAL-CHANGES; MOLECULAR-MECHANISM; NATRONOBACTERIUM-PHARAONIS; PHARAONIS PHOBORHODOPSIN; PROTON TRANSLOCATION; STRUCTURAL-CHANGES; TIME-RESOLVED DETECTION; TRANSIENT MOVEMENT; TRANSMEMBRANE HELICES
Erscheinungsdatum: 2004
Herausgeber: SPRINGERNATURE
Journal: PHOTOCHEMICAL & PHOTOBIOLOGICAL SCIENCES
Volumen: 3
Ausgabe: 6
Startseite: 543
Seitenende: 547
Zusammenfassung: 
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.
ISSN: 1474905X
DOI: 10.1039/b402656j

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