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

被引：20

作者：

Bordignon, Enrica

Klare, Johann P.

Holterhues, Julia

Martell, Swetlana

Krasnaberski, Aliaksei

Engelhard, Martin

Steinhoff, Heinz-Juergen ^{[1
]}

机构：

[1] Univ Osnabruck, Fachbereich Phys, D-4500 Osnabruck, Germany

[2] Max Planck Inst Mol Physiol, D-44139 Dortmund, Germany

来源：

PHOTOCHEMISTRY AND PHOTOBIOLOGY | 2007年 / 83卷 / 02期

关键词：

D O I：

10.1562/2006-07-05-RA-960

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：263 / 272

页数：10

共 34 条

[1] The M intermediate of Pharaonis phoborhodopsin is photoactive [J].