Ultrafast solvation dynamics at binding and active sites of photolyases.
Dynamic solvation at binding and active sites is critical to protein recognition and enzyme catalysis. We report here the complete characterization of ultrafast solvation dynamics at the recognition site of photoantenna molecule and at the active site of cofactor/substrate in enzyme photolyase by examining femtosecond-resolved fluorescence dynamics and the entire emission spectra. With direct use of intrinsic antenna and cofactor chromophores, we observed the local environment relaxation on the time scales from a few picoseconds to nearly a nanosecond. Unlike conventional solvation where the Stokes shift is apparent, we observed obvious spectral shape changes with the minor, small, and large spectral shifts in three function sites. These emission profile changes directly reflect the modulation of chromophore's excited states by locally constrained protein and trapped-water collective motions. Such heterogeneous dynamics continuously tune local configurations to optimize photolyase's function through resonance energy transfer from the antenna to the cofactor for energy efficiency and then electron transfer between the cofactor and the substrate for repair of damaged DNA. Such unusual solvation and synergetic dynamics should be general in function sites of proteins.
Department of Physics, Ohio State University, Columbus, OH 43210, USA.
Chih-Wei
CW
Chang
Lijun
L
Guo
Ya-Ting
YT
Kao
Jiang
J
Li
Chuang
C
Tan
Tanping
T
Li
Chaitanya
C
Saxena
Zheyun
Z
Liu
Lijuan
L
Wang
Aziz
A
Sancar
Dongping
D
Zhong
D002384:Catalysis; D020134:Catalytic Domain / Q000235:genetics; D004260:DNA Repair; D004255:Deoxyribodipyrimidine Photo-Lyase / Q000378:metabolism*; D005453:Fluorescence; D007700:Kinetics; D008958:Models, Molecular; D015394:Molecular Structure; D012997:Solvents / Q000378:metabolism*
D012997:Solvents; D004255:Deoxyribodipyrimidine Photo-Lyase