Literature summary for 4.1.99.13 extracted from

Li, J.; Uchida, T.; Ohta, T.; Todo, T.; Kitagawa, T.
Characteristic structure and environment in FAD cofactor of (6-4) photolyase along function revealed by resonance Raman spectroscopy (2006), J. Phys. Chem. B, 110, 16724-16732.

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Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Arabidopsis thaliana

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	-	-	-

Synonyms

Synonyms	Comment	Organism
(6-4) photolyase	-	Arabidopsis thaliana

Cofactor

Cofactor	Comment	Organism	Structure
FAD	Resonance Raman spectra of (6-4) photolyase having neutral semiquinoid and oxidized forms of FAD. Density functional theory (DFT) calculations are carried out on the neutral semiquinone. The marker band of a neutral semiquinone at 1606 cm-1 in H2O, splits into two comparable bands at 1594 and 1608 cm-1 in D2O, and similarly, that at 1522 cm-1 in H2O does into three bands at 1456, 1508, and 1536 cm-1 in D2O. This D2O effect is recognized only after being oxidized once and photoreduced to form a semiquinone again, but not by simple H/D exchange of solvent. Some Raman bands of the oxidized form are observed at significantly low frequencies (1621, 1576 cm-1) and with band splittings (1508/1493, 1346/1320 cm-1). These Raman spectral characteristics indicate strong H-bonding interactions (at N5-H, N1), a fairly hydrophobic environment, and an electron-lacking feature in benzene ring of the FAD cofactor, which seems to specifically control the reactivity of (6-4) photolyase	Arabidopsis thaliana

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Release 2023.1 (January 2023)