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

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
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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

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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, Royal Society of Chemistry, 2019, 21 (17), pp.8743-8756. ⟨10.1039/C8CP06072J⟩. ⟨hal-02095777⟩

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