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Literature summary for 4.1.99.13 extracted from

  • Cailliez, F.; Mueller, P.; Firmino, T.; Pernot, P.; de la Lande, A.
    Energetics of photoinduced charge migration within the tryptophan tetrad of an animal (6-4) photolyase (2016), J. Am. Chem. Soc., 138, 1904-1915 .
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(6-4) photoproduct (in DNA) Xenopus laevis
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2 pyrimidine residues (in DNA)
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Organism

Organism UniProt Comment Textmining
Xenopus laevis Q9I910
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Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(6-4) photoproduct (in DNA)
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Xenopus laevis 2 pyrimidine residues (in DNA)
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additional information polarizable molecular dynamics simulations and constrained density functional theory calculations reveal the energetics of charge migration along the tryptophan tetrad. Migration toward the fourth tryptophan is thermodynamically favorable. Electron transfer mechanisms occur either through an incoherent hopping mechanism or through a multiple sites tunneling process. The Jortner-Bixon formulation of electron transfer (ET) theory is employed to characterize the hopping mechanism, interplay between electron transfer and relaxation of protein and solvent, overview. Electron transfer in (6-4) photolyase proceeds out of equilibrium. Multiple site tunneling is modeled with the recently proposed flickering resonance mechanism Xenopus laevis ?
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Synonyms

Synonyms Comment Organism
(6-4) photolyase
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Xenopus laevis
animal (6-4) photolyase
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Xenopus laevis
Xl64phr
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Xenopus laevis

Cofactor

Cofactor Comment Organism Structure
FAD flavoprotein Xenopus laevis

General Information

General Information Comment Organism
evolution cryptochromes and photolyases are flavoproteins that undergo cascades of electron/hole transfers after excitation of the flavin cofactor. Animal (6-4) photolyases, as well as animal cryptochromes, feature a chain of four tryptophan residues, while other members of the family contain merely a tryptophan triad Xenopus laevis
additional information in Xenopus laevis (6-4) photolyase, the fourth residue of a chain of four tryptophan residues is effectively involved in photoreduction Xenopus laevis