DNA photolyase repairs UV-induced cyclobutylpyrimidine dimers in DNA using light-driven electron transfer from a FAD cofactor in the protein to the DNA molecule.   The enzyme is ubiquitous throughout the kingdom of life with the exception of placental mammals, and thus, is an important model to study how nature has adapted the enzyme to accommodate the different reaction conditions.  We have completed preliminary studies for the thermophilic S. solfataricus photolyase (SsPL) and the mesophilic E. coli photolyase (EcPL) proteins, examining both the thermodynamics of substrate binding and the ground state electrochemistry of the noncovalently bound FAD cofactors.   Differences between the mesophilic and thermophilic enzymes point to the interesting role that water plays in substrate binding.

DNA repair under extreme conditions: The redox chemistry and thermodynamics of substrate binding of an extremophilic DNA photolyase

248th National Meeting (2014)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.