Literature summary for 4.1.99.3 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.

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Activating Compound

Activating Compound	Comment	Organism	Structure
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)

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

Protein Variants

Protein Variants	Comment	Organism
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

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

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

Synonyms

Synonyms	Comment	Organism
DNA photolyase	-	Escherichia coli
photolyase	-	Escherichia coli

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Release 2023.1 (January 2023)