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
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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