Origin of the nonexponential dynamics of excited-state proton transfer in wt-green fluorescent protein.
We used an inhomogeneous excited-state proton-transfer kinetics model to explain the origin of the non-exponential time-resolved emission of the A-band of wt-green fluorescence protein. The calculated fit is rather good for both H 2O and D 2O samples in a wide temperature range of 80-229 K. We attribute the inhomogeneous kinetics to the distance dependence of the excited-state proton-transfer rate between the proton donor (the hydroxyl group of the chromophore) and the oxygen of a nearby water molecule.
Gepshtein
R
R
Raymond and Beverly Sackler Faculty of Exact Sciences, School of Chemistry, Tel Aviv University, Tel Aviv 69978, Israel.
Leiderman
P
P
Huppert
Dan
D
D000465:Algorithms; D017666:Deuterium Oxide / Q000737:chemistry; D005453:Fluorescence; D049452:Green Fluorescent Proteins / Q000737:chemistry*; D007700:Kinetics; D008956:Models, Chemical; D011522:Protons; D013050:Spectrometry, Fluorescence; D013696:Temperature; D014867:Water / Q000737:chemistry
D011522:Protons; C485192:green fluorescent protein, Aequorea victoria; D014867:Water; D049452:Green Fluorescent Proteins; D017666:Deuterium Oxide