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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geprüft am 15.05.2024