Abstract
Photolyases (PHRs) are DNA repair proteins that revert UV-induced photoproducts, either cyclobutane pyrimidine dimers (CPD) or (6-4) photoproducts (PPs), into normal bases to maintain genetic integrity. The (6-4) PHR must catalyze not only covalent bond cleavage but also hydroxyl or amino group transfer, yielding a more complex mechanism than that postulated for CPD PHR. Building upon recently established light-induced difference FTIR spectroscopy of Xenopus (6-4) PHR, we now utilize 15N3′-labeled (6-4) PP to identify vibrational modes of (6-4) PP upon repair. We successfully assign two and three vibrational bands for the (6-4) PP and the repaired thymine, respectively. Thus, the present FTIR spectroscopy is sensitive enough to distinguish a single nitrogen atom (15N versus 14N) among >6700 atoms in the enzyme–substrate complex.
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