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

Nadia Dozova; Fabien Lacombat; Charles Bou-Nader; Djemel Hamdane; Pascal Plaza

doi:10.1039/C8CP06072J

Journal articles

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, *}

* Corresponding author

1 PASTEUR - Processus d'Activation Sélective par Transfert d'Energie Uni-électronique ou Radiatif (UMR 8640)

2 LCPB - Laboratoire de Chimie des Processus Biologiques

Abstract : 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

Document type :

Journal articles

Domain :

Chemical Sciences / Theoretical and/or physical chemistry

Complete list of metadata

https://hal.archives-ouvertes.fr/hal-02095777
Contributor : Pascal Plaza <>
Submitted on : Monday, December 7, 2020 - 11:58:55 AM
Last modification on : Thursday, January 7, 2021 - 4:36:05 PM
Long-term archiving on: : Monday, March 8, 2021 - 6:48:41 PM

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

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

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