The emitting state of tryptophan in proteins with highly blue-shifted fluorescence

被引：33

作者：

Broos, Jaap

Tveen-Jensen, Karina

de Waal, Ellen

Hesp, Ben H.

Jackson, J. Baz

Canters, Gerard W.

Callis, Patrik R.

机构：

[1] Univ Groningen, Dept Biophys Chem, NL-9747 AG Groningen, Netherlands

[2] Univ Groningen, Dept Chem Phys, NL-9747 AG Groningen, Netherlands

[3] Univ Birmingham, Sch Biochem, Birmingham B15 2TT, W Midlands, England

[4] Leiden Univ, Inst Chem, NL-2333 CC Leiden, Netherlands

[5] Montana State Univ, Dept Chem & Biochem, Bozeman, MT 59717 USA

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2007年 / 46卷 / 27期

关键词：

azurin; fluorescence spectroscopy; protein structure; QM/MM calculations; tryptophan;

D O I：

10.1002/anie.200700839

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Kind of blue: Tryptophan residues embedded in rigid and hydrophobic protein matrices, like azurin and domain 1 of a transhydrogenase (dl), yield blue-shifted emission spectra with vibrational fine structure. These features are typical for emission from the 1Lb state of indole, and not the 1La state. Nevertheless, these proteins are found to emit from 1La, except for a mutant of domain 1 (dl.M97V), which features the most blue-shifted protein emission ever reported. (Graph Presented) © 2007 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：5137 / 5139

页数：3

共 16 条

[1] Tryptophan phosphorescence spectroscopy reveals that a domain in the NAD(H)-binding component (dI) of transhydrogenase from Rhodospirillum rubrum has an extremely rigid and conformationally homogeneous protein core [J].