BATHOIODOPSIN, A PRIMARY INTERMEDIATE OF IODOPSIN AT PHYSIOLOGICAL TEMPERATURE

被引：30

作者：

KANDORI, H ^{[1
]}

MIZUKAMI, T ^{[1
]}

OKADA, T ^{[1
]}

IMAMOTO, Y ^{[1
]}

FUKADA, Y ^{[1
]}

SHICHIDA, Y ^{[1
]}

YOSHIZAWA, T ^{[1
]}

机构：

[1] KYOTO UNIV,FAC SCI,DEPT BIOPHYS,KYOTO 606,JAPAN

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1990年 / 87卷 / 22期

关键词：

Color vision; Photoisomerization; Picosecond laser photolysis; Red-sensitive cone visual pigment;

D O I：

10.1073/pnas.87.22.8908

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Measurement of the primary photochemical reaction of iodopsin, a chicken red-sensitive cone visual pigment, was carried out at room temperature by using picosecond (ps) laser photolysis. Excitation of iodopsin with a ps green pulse (pulse width, 21 ps) caused the instantaneous formation of a bathochromic product, which was stable on a ps time scale. This product may correspond to "bathoiodopsin," which was detected by low-temperature spectrophotometry. Although bathoiodopsin produced at the temperature of liquid nitrogen or helium reverted to the original pigment (iodopsin) on warming (above -170°C), the bathoiodopsin produced at physiological temperature decayed to all-trans-retinal and R-photopsin (the protein moiety of iodopsin) presumably through several intermediates. The absorption maximum of bathoiodopsin at room temperature was at 625 nm, a wavelength slightly shorter than that measured at low temperature (λmax, 640 nm). The extinction coefficient of bathoiodopsin at room temperature was lower than that at low temperature and close to that of the original iodopsin at room temperature.

引用

页码：8908 / 8912

页数：5

共 22 条

[1]

BAYLOR DA, 1982, METHOD ENZYMOL, V81, P403

[2] VISUAL PIGMENTS IN SINGLE RODS + CONES OF HUMAN RETINA - DIRECT MEASUREMENTS REVEAL MECHANISMS OF HUMAN NIGHT + COLOR VISION [J].