Ultrafast solvation dynamics at binding and active sites of photolyases

• DOI: 10.1073/pnas.1000001107
• Publication Date: 2010-01-27T04:49:26Z
• Authors: Chih-Wei Chang; Lijun Guo; Ya-Ting Kao; Jiang Li; Chuang Tan; Tanping Li; Chaitanya Saxena; Zheyun Liu; Lijuan Wang; Aziz Sancar; Dongping Zhong
• Keywords: Photolyase; Protein Dynamics; Chromophore

Dynamic solvation at binding and active sites is critical to protein recognition enzyme catalysis. We report here the complete characterization of ultrafast dynamics site photoantenna molecule cofactor/substrate in photolyase by examining femtosecond-resolved fluorescence entire emission spectra. With direct use intrinsic antenna cofactor chromophores, we observed local environment relaxation on time scales from a few picoseconds nearly nanosecond. Unlike conventional where Stokes shift apparent, obvious spectral shape changes with minor, small, large shifts three function sites. These profile directly reflect modulation chromophore’s excited states locally constrained trapped-water collective motions. Such heterogeneous continuously tune configurations optimize photolyase’s through resonance energy transfer for efficiency then electron between substrate repair damaged DNA. unusual synergetic should be general proteins.