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Literature summary for 4.1.99.3 extracted from

  • Kodali, G.; Siddiqui, S.U.; Stanley, R.J.
    Charge redistribution in oxidized and semiquinone E. coli DNA photolyase upon photoexcitation: stark spectroscopy reveals a rationale for the position of Trp382 (2009), J. Am. Chem. Soc., 131, 4795-4807.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Escherichia coli P00914
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Storage Stability

Storage Stability Organism
-80°C, 50% glycerol Escherichia coli

Synonyms

Synonyms Comment Organism
DNA photolyase
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FAD critical W382 residue relative to the flavin for efficient vectorial electron transfer leading to photoreduction Escherichia coli
FADH2
-
Escherichia coli
methenyltetrahydrofolate
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Escherichia coli
additional information light-driven blue light flavophotoreceptors all operate from the excited state, whether singlet oxidized (e.g., BLUF and LOV domains) or doublet semiquinone Escherichia coli