Natural and non-natural antenna chromophores in the DNA photolyase from Thermus Thermophilus

Tobias Klar, Gebhard Kaiser, Ulrich Hennecke, Thomas Carell, Alfred Batschauer, Lars Oliver Essen

Research output: Contribution to journalArticle

42 Citations (Scopus)

Abstract

X-ray crystallographic and functional analysis of the class I DNA photolyase from Thermus thermophilus revealed the binding of flavin mononucleotide (FMN) as an antenna chromophore. The binding mode of FMN closely coincides with the binding of a deazaflavin-like chromophore in the related class I DNA photolyase from Anacystis nidulans. Compared to the R46E mutant, which lacks a conserved arginine in the binding site for the antenna chromophore, the FMN-comprising holophotolyase exhibits an eightfold higher activity at 450 nm. The facile incorporation of the flavin cofactors 8-hydroxy-deazariboflavin and 8-iodo-8-demethyl-riboflavin into the binding site for the antenna chromophore paves the way for wavelength-tuning of the activity spectra of DNA photolyases by using synthetic flavins.

Original languageEnglish
Pages (from-to)1798-1806
Number of pages9
JournalChemBioChem
Volume7
Issue number11
DOIs
Publication statusPublished - 1 Nov 2006

Keywords

  • Chromophores
  • DNA repair
  • Enzyme catalysis
  • Flavins
  • Photocatalysis
  • Protein structures

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