Flavoproteins are unique redox coenzymes and the dynamic solvation at their function sites is critical to the understanding of their biological activities. Using intrinsic flavin cofactor as the local optical probes with site-specific mutations, we systematically studied two important proteins, a mode redox protein of flavodoxin and a critical DNA-repair photoenzyme of photolyase, and observed distinct ultrafast solvation dynamics on multiple time scales in different redox states and in different binding and active sites. These dynamics can be directly related to their local biological water properties and structural flexibility and have an intimate relationship with biological functions.

Ultrafast solvation dynamics at binding and active sites of proteins

243rd National Meeting (2012)

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