Ultrafast dynamics of protein proton transfer on short hydrogen bond potential energy surfaces: S65T/H148D GFP.
Ultrafast proton transfer dynamics on a short H-bond in a protein were studied through the time-resolved fluorescence of the S65T/H148D green fluorescent protein (GFP) mutant. In response to the change in chromophore pK(a) upon excitation, the donor-proton-acceptor structure evolves on a sub-100 fs time scale, followed by picosecond time scale vibrational cooling and host structure reorganization.
Kondo
Minako
M
School of Chemistry, University of East Anglia, Norwich NR4 7TJ, UK.
Heisler
Ismael A
IA
Stoner-Ma
Deborah
D
Tonge
Peter J
PJ
Meech
Stephen R
SR
D049452:Green Fluorescent Proteins / Q000032:analysis* / Q000235:genetics; D006860:Hydrogen Bonding; D008958:Models, Molecular; D050505:Mutant Proteins / Q000032:analysis / Q000235:genetics; D011522:Protons; D013050:Spectrometry, Fluorescence
D050505:Mutant Proteins; D011522:Protons; D049452:Green Fluorescent Proteins