PHOTOAFFINITY-LABELING OF RHODOPSIN AND BACTERIORHODOPSIN

被引：31

作者：

NAKANISHI, K ^{[1
]}

ZHANG, HZ ^{[1
]}

LERRO, KA ^{[1
]}

TAKEKUMA, S ^{[1
]}

YAMAMOTO, T ^{[1
]}

LIEN, TH ^{[1
]}

SASTRY, L ^{[1
]}

BAEK, DJ ^{[1
]}

MOQUINPATTEY, C ^{[1
]}

BOEHM, MF ^{[1
]}

DERGUINI, F ^{[1
]}

GAWINOWICZ, MA ^{[1
]}

机构：

[1] COLUMBIA UNIV,COLL PHYS & SURG,NEW YORK,NY 10027

来源：

BIOPHYSICAL CHEMISTRY | 1995年 / 56卷 / 1-2期

关键词：

RHODOPSIN; BACTERIORHODOPSIN; PHOTOAFFINITY LABELING; RHODOPSIN (CHROMOPHORE LOCATION); LOCKED RETINAL ANALOG; SIDE-CHAIN METHYLS;

D O I：

10.1016/0301-4622(95)00010-U

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：

Photoaffinity labeling with bovine rhodopsin using a retinal with a fixed 11-cis-ene cross-linked exclusively to Trp-265/Leu-266 in helix F, showing that the beta-ionone C-3 is close to helix F. Moreover, since these labeled amino acids are in the middle of helix F, while the Schiff-base linkage to Lys-296 at the other terminus of the chromophore is also in the middle of helix G, the chromophore lies horizontally near the center of the lipid bilayer. In bacteriorhodopsin, photoaffinity studies using a retinal with a C-10 tritiated phenylazide appended through a 13 Angstrom spacer cross-linked to Arg-175/Asn-176 on the cytoplasmic side of helix F; this indicates that 9-Me points toward the extracellular space. This result agrees with our earlier studies with 9-sulfate analogs but is opposite to that deduced by biophysical measurements.

引用

页码：13 / 22

页数：10

共 42 条

[1] A COMPARATIVE-STUDY OF THE INFRARED DIFFERENCE SPECTRA FOR OCTOPUS AND BOVINE RHODOPSINS AND THEIR BATHORHODOPSIN PHOTOINTERMEDIATES [J].