Ultrafast photoinduced flavin dynamics in the unusual active site of the tRNA methyltransferase TrmFO
Résumé
Flavoproteins often stabilize their flavin coenzyme by stacking interactions involving the isoalloxazine moiety of the flavin and an aromatic residue from the apoprotein. The bacterial FAD and folate-dependent tRNA methyltransferase TrmFO has the singularity of stabilizing its FAD coenzyme by an unusual H-bond-assisted - stacking interaction, involving a conserved tyrosine (Y 346 in Bacillus subtilis TrmFO, BsTrmFO), the isoalloxazine of FAD and the backbone of a catalytic
Domaines
Chimie théorique et/ou physique
Origine : Fichiers produits par l'(les) auteur(s)