Proton relay reaction in green fluorescent protein (GFP): Polarization-resolved ultrafast vibrational spectroscopy of isotopically edited GFP.
The complex transient vibrational spectra of wild type (wt) GFP have been assigned through polarization anisotropy measurements on isotopically edited proteins. Protein chromophore interactions modify considerably the vibrational structure, compared to the model chromophore in solution. An excited-state vibrational mode yields information on excited-state electronic structure. The proton relay pathway is characterized in more detail, and the protonation of the remote E222 residue is shown to occur in a concerted step. Modifications to protein vibrational modes are shown to occur following electronic excitation, and the potential for these to act as a trigger to the proton relay reaction is discussed.
Stoner-Ma
Deborah
D
Department of Chemistry, Stony Brook University, Stony Brook, New York 11794-3400, USA.
Melief
Edward H
EH
Nappa
Jérôme
J
Ronayne
Kate L
KL
Tonge
Peter J
PJ
Meech
Stephen R
SR
D004926:Escherichia coli / Q000378:metabolism; D049452:Green Fluorescent Proteins / Q000737:chemistry*; D006860:Hydrogen Bonding; D010957:Plasmids; D011487:Protein Conformation; D011522:Protons; D013057:Spectrum Analysis / Q000379:methods*
D011522:Protons; D049452:Green Fluorescent Proteins