Analysis of light-induced conformational changes of Natronomonas pharaonis sensory rhodopsin II by time resolved electron paramagnetic resonance spectroscopy

Autor(en): Bordignon, Enrica
Klare, Johann P.
Holterhues, Julia
Martell, Swetlana
Krasnaberski, Aliaksei
Engelhard, Martin
Steinhoff, Heinz-Juergen 
Stichwörter: BACTERIORHODOPSIN; Biochemistry & Molecular Biology; Biophysics; COGNATE TRANSDUCER; HELIX-F; HIGH-FIELD EPR; NATRONOBACTERIUM-PHARAONIS; PHOBORHODOPSIN; PROTON TRANSLOCATION; RECEPTOR; STRUCTURAL-CHANGES; TRANSIENT MOVEMENT
Erscheinungsdatum: 2007
Herausgeber: WILEY
Journal: PHOTOCHEMISTRY AND PHOTOBIOLOGY
Volumen: 83
Ausgabe: 2
Startseite: 263
Seitenende: 272
Zusammenfassung: 
The nature and kinetics of the conformational changes leading to the activated state of NpSRII/NpHtrII(157) were investigated by time-resolved electron paramagnetic resonance (TR-EPR) spectroscopy in combination with site-directed spin labeling (SDSL) on a series of spin labeled mutants of NpSRII. A structural rearrangement of the cytoplasmic moiety of NpSRII upon light activation was detected (helices B, C, F and G). The increase in distance between helices C and F in the M-trapped state of the complex observed in one double mutant is in line with the notion that an outward movement of helix F occurs upon receptor activation. The data obtained from the NpSRII/NpHtrII(157) complex reconstituted in purple membrane lipids are compared with those obtained from the X-ray structure of the late M-state of the complex which shows some discrepancies. The results are discussed in the context also of other biophysical and EPR experimental evidences.
Beschreibung: 
12th International Conference on Retinal Proteins, Awaji Isl, JAPAN, JUN 04-08, 2006
ISSN: 00318655
DOI: 10.1562/2006-07-05-RA-960

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