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Significant Expansion of the Fluorescent Protein Chromophore through the Genetic Incorporation of a Metal‐Chelating Unnatural Amino Acid
Author(s) -
Liu Xiaohong,
Li Jiasong,
Hu Cheng,
Zhou Qing,
Zhang Wei,
Hu Meirong,
Zhou Juanzuo,
Wang Jiangyun
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201301307
Subject(s) - chromophore , fluorescence , fluorescent protein , chelation , amino acid , chemistry , metal , green fluorescent protein , biochemistry , photochemistry , organic chemistry , gene , physics , quantum mechanics
Caught red‐shifted : A novel metal‐chelating unnatural amino acid with an 8‐hydroxyquinoline group (HqAla) can be enzymatically incorporated into GFP (see scheme). Substituting a Tyr residue in the chromophore of FPs with HqAla results in significantly red‐shifted excitation and emission maxima. The crystal structure of superfolder GFP bearing HqAla in its chromophore shows the structural basis for these red shifts.