Ultrafast photoinduced flavin dynamics in the unusual active site of the tRNA methyltransferase TrmFO

Nadia Dozova (1) , Fabien Lacombat (1) , Charles Bou-Nader (2) , Djemel Hamdane (2) , Pascal Plaza (1)

1 PASTEUR - Processus d'Activation Sélective par Transfert d'Energie Uni-électronique ou Radiatif (UMR 8640)
2 LCPB - Laboratoire de Chimie des Processus Biologiques

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

Nadia Dozova, Fabien Lacombat, Charles Bou-Nader, Djemel Hamdane, Pascal Plaza. Ultrafast photoinduced flavin dynamics in the unusual active site of the tRNA methyltransferase TrmFO. Physical Chemistry Chemical Physics, 2019, 21 (17), pp.8743-8756. ⟨10.1039/C8CP06072J⟩. ⟨hal-02095777⟩