RESUMEN
Pyridoxal phosphate (PLP) was found to deactivate triplet-excited riboflavin (Rib) in aqueous solution with a deactivation constant of 3.0 ± 0.1 × 10(8) L mol(-1) s(-1) at 25 °C. Likewise, PLP was found to quench the fluorescence emission of (1)Rib* with (1)kq = 1.0 ± 0.1 × 10(11) L mol(-1) s(-1) as determined by steady state fluorescence. The rather high quenching constant suggests the formation of a ground state complex, which was further confirmed by time-resolved fluorescence measurements to yield a (1)Rib* deactivation constant of 3.4 ± 0.4 × 10(10) L mol(-1) s(-1). Triplet quenching is assigned as one-electron transfer rather than hydrogen-atom transfer from PLP to (3)Rib*, as the reaction quantum yield, Φ = 0.82, is hardly influenced by solvent change from water to D2O, Φ = 0.78. Neither biotin nor niacin deactivates the singlet- or triplet-excited riboflavin as it is expected from their higher oxidation potentials E > 2 V vs NHE.