Ultrafast electronic and vibrational dynamics of stabilized A state mutants of the green fluorescent protein (GFP): Snipping the proton wire

被引：13

作者：

Stoner-Ma, Deborah ^{[1
]}

Jaye, Andrew A. ^{[1
]}

Ronayne, Kate L. ^{[2
]}

Nappa, Jerome ^{[3
]}

Tonge, Peter J. ^{[1
]}

Meech, Stephen R. ^{[3
]}

机构：

[1] SUNY Stony Brook, Dept Chem, Stony Brook, NY 11794 USA

[2] Rutherford Appleton Lab, Cent Laser Facil, Sci & Technol Facil Council, Didcot OX11 0QX, Oxon, England

[3] Univ E Anglia, Sch Chem Sci & Pharm, Norwich NR4 7TJ, Norfolk, England

来源：

CHEMICAL PHYSICS | 2008年 / 350卷 / 1-3期

关键词：

ultrafast; transient infra-red; green fluorescent protein; proton transfer; fluorescence; protein dynamics; fluorescent protein;

D O I：

10.1016/j.chemphys.2008.02.021

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Two blue absorbing and emitting mutants (S65G/T203V/E222Q and S65T at pH 5.5) of the green fluorescent protein (GFP) have been investigated through ultrafast time resolved infra-red (TRIR) and fluorescence spectroscopy. In these mutants, in which the excited state proton transfer reaction observed in wild-type GFP has been blocked, the photophysics are dominated by the neutral A state. It was found that the A* excited state lifetime is short, indicating that it is relatively less stabilised in the protein matrix than the anionic form. However, the lifetime of the A state can be increased through modifications to the protein structure. The TRIR spectra show that a large shifts in protein vibrational modes on excitation of the A state occurs in both these GFP mutants. This is ascribed to a change in H-bonding interactions between the protein matrix and the excited state. (C) 2008 Elsevier B.V. All rights reserved.

引用

页码：193 / 200

页数：8

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