Characterisation of Schiff base and chromophore in green proteorhodopsin by solid-state NMR

被引：47

作者：

Pfleger, Nicole ^{[1
]}

Lorch, Mark ^{[1
]}

Woerner, Andreas C. ^{[1
]}

Shastri, Sarika ^{[1
]}

Glaubitz, Clemens ^{[1
]}

机构：

[1] Goethe Univ Frankfurt, Ctr Biomol Magnet Resonance, Inst Biophys Chem, D-60438 Frankfurt, Germany

来源：

JOURNAL OF BIOMOLECULAR NMR | 2008年 / 40卷 / 01期

基金：

英国工程与自然科学研究理事会;

关键词：

proteorhodopsin; solid-state NMR; Schiff base; retinal;

D O I：

10.1007/s10858-007-9203-5

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：

The proteorhodopsin family consists of hundreds of homologous retinal containing membrane proteins found in bacteria in the photic zone of the oceans. They are colour tuned to their environment and act as light-driven proton pumps with a potential energetic and regulatory function. Precise structural details are still unknown. Here, the green proteorhodopsin variant has been selected for a chemical shift analysis of retinal and Schiff base by solid-state NMR. Our data show that the chromophore exists in mainly all-trans configuration in the proteorhodopsin ground state. The optical absorption maximum together with retinal and Schiff base chemical shifts indicate a strong interaction network between chromophore and opsin.

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页码：15 / 21

页数：7

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