A light-driven sodium ion pump in marine bacteria

被引：321

作者：

Inoue, Keiichi ^{[1
,2
]}

Ono, Hikaru ^{[1
]}

Abe-Yoshizumi, Rei ^{[1
]}

Yoshizawa, Susumu ^{[3
]}

Ito, Hiroyasu ^{[1
]}

Kogure, Kazuhiro ^{[3
]}

Kandori, Hideki ^{[1
]}

机构：

[1] Nagoya Inst Technol, Dept Frontier Mat, Showa Ku, Nagoya, Aichi 4668555, Japan

[2] Japan Sci & Technol Agcy, PRESTO, Kawaguchi, Saitama 3320012, Japan

[3] Univ Tokyo, Atmosphere & Ocean Res Inst, Kashiwa, Chiba 2778564, Japan

来源：

NATURE COMMUNICATIONS | 2013年 / 4卷

关键词：

RETINAL SCHIFF-BASE; BACTERIORHODOPSIN MUTANTS; PROTON TRANSLOCATION; STRUCTURAL-CHANGES; PROTEORHODOPSIN; HALORHODOPSIN; SUBSTITUTIONS; PHOTOCYCLE; RHODOPSIN; TRANSPORT;

D O I：

10.1038/ncomms2689

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：

Light-driven proton-pumping rhodopsins are widely distributed in many microorganisms. They convert sunlight energy into proton gradients that serve as energy source of the cell. Here we report a new functional class of a microbial rhodopsin, a light-driven sodium ion pump. We discover that the marine flavobacterium Krokinobacter eikastus possesses two rhodopsins, the first, KR1, being a prototypical proton pump, while the second, KR2, pumps sodium ions outward. Rhodopsin KR2 can also pump lithium ions, but converts to a proton pump when presented with potassium chloride or salts of larger cations. These data indicate that KR2 is a compatible sodium ion-proton pump, and spectroscopic analysis showed it binds sodium ions in its extracellular domain. These findings suggest that light-driven sodium pumps may be as important in situ as their proton-pumping counterparts.

引用

页数：10

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