Photoswitching of the fluorescent protein asFP595:: Mechanism, proton pathways, and absorption spectra

被引：89

作者：

Schaefer, Lars V.

Groenhof, Gerrit

Klingen, Astrid R.

Ullmann, G. Matthias

Boggio-Pasqua, Martial

Robb, Michael A.

Grubmueller, Helmut

机构：

[1] Max Planck Inst Biophys Chem, Abt Theoret & Comp Gestutzte Biophys, D-37077 Gottingen, Germany

[2] Univ Bayreuth, Abt Strukturbiol Bioinformat, D-95447 Bayreuth, Germany

[3] Univ London Imperial Coll Sci Technol & Med, Dept Chem, London SW7 2AZ, England

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2007年 / 46卷 / 04期

基金：

英国工程与自然科学研究理事会;

关键词：

absorption spectroscopy; isomerization; molecular dynamics; proteins; proton transport;

D O I：

10.1002/anie.200602315

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

(Figure Presented) Molecular light-switch: Off-on switching of the fluorescence of the protein asFP595 involves a trans-cis isomerization. Mixed quantum/classical simulations elucidate the spectroscopic properties of asFP595 and give detailed insights into the photoswitching mechanism. The conformational trans-cis switching triggers a proton-transfer cascade between the chromophore and adjacent amino acids. © 2007 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

收藏

页码：530 / 536

页数：7

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