Tyrosine structural changes detected during the photoactivation of rhodopsin

被引:34
作者
DeLange, F
Klaassen, CHW
Wallace-Williams, SE
Bovee-Geurts, PHM
Liu, XM
DeGrip, WJ
Rothschild, KJ
机构
[1] Boston Univ, Dept Phys, Boston, MA 02215 USA
[2] Boston Univ, Lab Mol Biophys, Boston, MA 02215 USA
[3] Univ Nijmegen, Dept Biochem, Inst Cellular Signalling, NL-6500 HB Nijmegen, Netherlands
关键词
D O I
10.1074/jbc.273.37.23735
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
We present the first Fourier transform infrared (FTIR) analysis of an isotope-labeled eukaryotic membrane protein. A combination of isotope labeling and FTIR difference spectroscopy was used to investigate the possible involvement of tyrosines in the photoactivation of rhodopsin (Rho), Rho --> MII difference spectra were obtained at 10 degrees C for unlabeled recombinant Rho and isotope-labeled L-[ring-(2)H(4)]Tyr-Rho expressed in Spodoptera frugiperda cells grown on a stringent culture medium containing enriched L-[ring-(2)H(4)]Tyr and isolated using a His, tag, A comparison of these difference spectra revealed reproducible changes in bands that correspond to tyrosine and tyrosinate vibrational modes. A similar pattern of tyrosine/tyrosinate bands has also been observed in the bR --> M transition in bacteriorhodopsin, although the sign of the bands is reversed. In bacteriorhodopsin, these bands were assigned to Tyr-185, which along with Pro-186 in the F-helix, may form a hinge that facilitates alpha-helix movement.
引用
收藏
页码:23735 / 23739
页数:5
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