Flavin mononucleotide (FMN) is a highly efficient photosensitizer
First-pass extracted concept
flavin mononucleotide
Aliases
FMN
Evidence Snippets
The extended time scale and wavenumber range allowed us to monitor the complete excited-state dynamics of the biological chromophore flavin mononucleotide (FMN), both free in solution and embedded in two variants of the bacterial light-oxygen-voltage (LOV) photoreceptor EL222.
a flavin mononucleotide (FMN) cofactor
the flavin mononucleotide (FMN) cofactor
Supporting Sources
Linked Claims
AsLOV2 can be used as a vehicle for FMN photosensitizer release triggered by light irradiation.
to utilize AsLOV2, due to its inherent binding propensity to FMN, as a PS vehicle, which is released at a target by light irradiation
Observed lifetimes and intermediate states including singlet, triplet, and adduct agree with previous time-resolved infrared spectroscopy experiments.
The observed lifetimes and intermediate states (singlet, triplet, and adduct) are in agreement with previous time-resolved infrared spectroscopy experiments.
The extended time scale and wavenumber range allowed monitoring of the complete excited-state dynamics of FMN free in solution and FMN embedded in two EL222 variants.
The extended time scale and wavenumber range allowed us to monitor the complete excited-state dynamics of the biological chromophore flavin mononucleotide (FMN), both free in solution and embedded in two variants of the bacterial light-oxygen-voltage (LOV) photoreceptor EL222.
A weak long-lived emission component from 600 to 650 nm in LOV2 was assigned to phosphorescence from the reactive FMN triplet state.
A weak long-lived component with emission intensity from 600 to 650 nm was assigned to phosphorescence from the reactive FMN triplet state.
FMN in aqueous solution showed pH-dependent fluorescence lifetimes of 2.7 ns at pH 2 and 3.9-4.1 ns at pH 3-8.
FMN dissolved in aqueous solution showed pH-dependent fluorescence lifetimes of 2.7 ns at pH 2 and 3.9-4.1 ns at pH 3-8.
Phototropin light-dependent action is based on reversible formation of a covalent bond between an FMN cofactor and a conserved cysteine in LOV domains.
The phototropins are blue-light receptors that base their light-dependent action on the reversible formation of a covalent bond between a flavin mononucleotide (FMN) cofactor and a conserved cysteine in light, oxygen or voltage (LOV) domains.
Cryogenic-temperature ENDOR spectroscopy can be applied to LOV domains to gain information on the direct vicinity of the FMN cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN isoalloxazine ring.
we describe how cryogenic-temperature ENDOR spectroscopy can be applied to various LOV domains ... to gain information on the direct vicinity of the flavin mononucleotide (FMN) cofactor by analyzing the temperature dependence of methyl-group rotation attached to C(8) of the FMN's isoalloxazine ring