EQUILIBRIUM COMPOSITION OF RETINAL ISOMERS IN DARK-ADAPTED BACTERIORHODOPSIN AND EFFECT OF HIGH-PRESSURE PROBED BY NEAR-INFRARED RAMAN-SPECTROSCOPY

被引:13
作者
SCHULTE, A [1 ]
BRADLEY, L [1 ]
WILLIAMS, C [1 ]
机构
[1] UNIV CENT FLORIDA,CTR RES EDUC OPT & LASERS,ORLANDO,FL 32816
关键词
CHROMOPHORE ISOMERIZATION; PURPLE MEMBRANE; LIGHT ADAPTATION; PROTEIN VOLUME CHANGE;
D O I
10.1366/0003702953963265
中图分类号
TH7 [仪器、仪表];
学科分类号
0804 ; 080401 ; 081102 ;
摘要
The combination of near-infrared Raman spectroscopy and variations in external parameters offers new opportunities for site-specific studies of proteins. Using excitation at 840 nm, we have measured the near-infrared Raman spectrum of dark-adapted bacteriorhodopsin at ambient and high pressure. The C=C ethylenic stretching region shows two resolved bands at 1526 and 1534 cm(-1), corresponding to the all-trans and 13-cis isomers. From deconvolution of these bands we find an isomeric ratio between 13-cis and all-trans retinal equal to 1 at ambient pressure. The Raman spectrum gives direct spectroscopic evidence that the 13-cis component is favored at high pressure, implying that it has a smaller volume. The pressure dependence of the isomeric ratio yields a molar volume of -6.6 mL/mol, which suggests ionization of one or two residues or the formation of three hydrogen bonds.
引用
收藏
页码:80 / 83
页数:4
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