Biophysics and Physicobiology

The Biophysical Society of Japan.

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FTIR study of light-dependent DNA repair processes in (6-4) photolyase histidine mutants.

Comparison of the light-induced difference Fourier transform infrared (FTIR) spectra of Xenopus (6-4) photolyase (PHR) for the wild type (black line), H354A mutant (red line), and H358A mutant (blue line). A vertical axis is scaled in 0.01 absorbance units. These spectra show the DNA repair process, namely (6-4) photoproduct to two thymines (top left). Previous mutation analysis revealed that H354A had no repair activity, while H358A had slight repair activity, however, similarity in the difference of FTIR spectra between the wild type and mutant proteins suggest that both mutants still maintain their repair activity. The mutation sites in (6-4) photoproduct binding site of (6-4) PHR are shown on the structure (PDB: 3CVU) at the bottom right. The amino acid residue number is based on the sequence of Xenopus (6-4) PHR. See Yamada, D. et al. Biophysics and Physicobiology, 12, 139-144 (2015).

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