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Literature summary extracted from

  • Byrdin, M.; Lukacs, A.; Thiagarajan, V.; Eker, A.P.; Brettel, K.; Vos, M.H.
    Quantum yield measurements of short-lived photoactivation intermediates in DNA photolyase: toward a detailed understanding of the triple tryptophan electron transfer chain (2010), J. Phys. Chem. A, 114, 3207-3214.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.1.99.3 FADH2 in wild-type, substantial losses occur prior to formation of the ultimate (FADH- 306TrpH°+) charge pair but that there is no significant kinetic development in the 100 ps-to-10 ns time window. The quantum yield of FADH- W306°+ is at 19%, in reference to the established quantum yield of the long-lived excited state of [Ru(bpy)3]2+ Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.99.3 wild-type and mutant Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
4.1.99.3 W306F lacks the ultimate intrinsic electron donor (terminal tryptophan replaced by redox inert phenylalanine), shows an important deprotonation/recombination process with a time constant of 0.85 ns Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.1.99.3 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.99.3 wild-type and mutant Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
4.1.99.3 DNA photolyase
-
 Escherichia coli
4.1.99.3 photolyase
-
 Escherichia coli