2.1.1.74	FAD	contains tightly bound flavin	676202	
2.1.1.74	FAD	dependent on	701488	
2.1.1.74	FAD	dependent on, recognition and binding structure, overview	706541	
2.1.1.74	FADH2	-	485582, 485583, 671555	
2.1.1.74	FADH2	using spectroscopic characterization it is shown that TrmFO stabilizes the protonated semiquinone FADH and a catalytic intermediate containing most likely both methylenetetrahydrofolate and an FAD reduced form. TrmFO, in the absence of tRNA, maintains an insulated active site that locks up the methyl donor and protects the reduced forms of the flavin from deleterious oxidative reactions	718903	
2.1.1.74	NADH	is used in the assay as electron donor	720967	
2.1.1.74	NADPH	-	485581