TY - JOUR
T1 - Protonation effects on the chromophore of green fluorescent protein. Quantum chemical study of the absorption spectrum
AU - Voityuk, Alexander A.
AU - Michel-Beyerle, Maria Elisabeth
AU - Rösch, Notker
N1 - Funding Information:
This work has been supported by the Deutsche Forschungsgemeinschaftv ia SFB 377 and by the Fonds der Chemischen Industrie.
PY - 1997/6/27
Y1 - 1997/6/27
N2 - The absorption spectrum of the chromophore of the green fluorescent protein (GFP) was investigated by INDO/S-CI model calculations. Geometrical variations of the hydrogen bonds between the chromophore and its environment were studied in detail. Based on the good agreement between experimental and calculated data, the spectrum of GFP is assigned. The absorptions at 397 and 477 nm are due to the chromophore cation and zwitterion, respectively. The phenolic oxygen of the chromophore is deprotonated in the excited state, but can be protonated or deprotonated in the ground state. The heterocyclic nitrogen remains protonated after excitation.
AB - The absorption spectrum of the chromophore of the green fluorescent protein (GFP) was investigated by INDO/S-CI model calculations. Geometrical variations of the hydrogen bonds between the chromophore and its environment were studied in detail. Based on the good agreement between experimental and calculated data, the spectrum of GFP is assigned. The absorptions at 397 and 477 nm are due to the chromophore cation and zwitterion, respectively. The phenolic oxygen of the chromophore is deprotonated in the excited state, but can be protonated or deprotonated in the ground state. The heterocyclic nitrogen remains protonated after excitation.
UR - http://www.scopus.com/inward/record.url?scp=0031587905&partnerID=8YFLogxK
U2 - 10.1016/S0009-2614(97)88003-7
DO - 10.1016/S0009-2614(97)88003-7
M3 - Article
AN - SCOPUS:0031587905
SN - 0009-2614
VL - 272
SP - 162
EP - 167
JO - Chemical Physics Letters
JF - Chemical Physics Letters
IS - 3-4
ER -