title: Ultrafast dynamics of protein proton transfer on short hydrogen bond potential energy surfaces: S65T/H148D GFP.
abstract: 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.
authors.affiliation: School of Chemistry, University of East Anglia, Norwich NR4 7TJ, UK.
authors.forename: Minako
authors.initials: M
authors.lastname: Kondo
authors.forename: Ismael A
authors.initials: IA
authors.lastname: Heisler
authors.forename: Deborah
authors.initials: D
authors.lastname: Stoner-Ma
authors.forename: Peter J
authors.initials: PJ
authors.lastname: Tonge
authors.forename: Stephen R
authors.initials: SR
authors.lastname: Meech
mesh_terms: 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
chemical_list: D050505:Mutant Proteins; D011522:Protons; D049452:Green Fluorescent Proteins