Spectroscopy and Photophysics of Lumiflavins and Lumichromes

Sikorska, Ewa; Khmelinskii, Igor; Prukała, Wiesław; Williams, Siân L.; Patel, Manisha J.; Worrall, David R.; Bourdelande, J. L.; Koput, and Jacek; Sikorski, Marek

doi:10.1021/jp037048u

Cited by 131 publications

(152 citation statements)

References 39 publications

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“…It has been reported that this first band is not much affected by polarity or the hydrogen bond of the solvent. 8,9 The pictures of MOs in Figure 5 may give an insight as to why the first ? * transition (HOMO ?…”

Section: Electronic Spectrum Of Lumiflavinmentioning

confidence: 99%

Theoretical study of the electronic spectra of oxidized and reduced states of lumiflavin and its derivative

2007

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Time-dependent density functional theory has been applied to investigate the electronic absorption spectrum of oxidized and reduced lumiflavin and its derivative, 8-NH(2)-lumiflavin. The calculations allow the authors to explain the origin of the difference in spectral features between oxidized and reduced states of lumiflavin. For the reduced lumiflavin, a reasonable assignment of the experimental spectrum has been made for the first time. Furthermore, the results obtained reveal that the NH(2) group plays a critical role in shaping the spectral features of 8-NH(2)-lumiflavin, and offer a reasonable explanation for the spectral changes upon substituting the NH(2) group for the CH(3) group of lumiflavin.

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Section: Electronic Spectrum Of Lumiflavinmentioning

confidence: 99%

Theoretical study of the electronic spectra of oxidized and reduced states of lumiflavin and its derivative

2007

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“…5) 32 as the masking ligand in the competitive binding system, where the well-separated emission wavelength of lumiflavin (λem = 530 nm) 32 compared to alloxazine (λem = 453 nm) is considered to be appropriate although lumiflavin shows the fluorescence to a certain degree (ffl = 0.14). 31 In the absence of lumiflavin, the most significant fluorescence quenching of alloxazine was obtained for A opposite an AP site in the DNA duplexes, but alloxazine also shows the large response to T. In the competitive binding with lumiflavin, the alloxazine binding to T was effectively blocked due to the strong binding of lumiflavin to T opposite the AP site, which results in the decrease in the fluorescence response of alloxazine to T (Fig. 5).…”

Section: Resultsmentioning

confidence: 99%

“…29,30 In addition, Lch shows fluorescence emission with a maximum at 475 nm that is separated from the emission of ATMND (λem = 405 nm), and shows low fluorescence quatum yield (ffl = 0.088). 31 It is thus expected that Lch effectively inhibits ATMND binding to T without interfering with the binding of ATMND to C. Actually, fluorescence signaling of ATMND is less influenced in the presence of Lch. Enhanced base-discrimination efficiency based on competitive binding of ATMND and Lch at the AP site was discussed as a simple and effective approach to develop AP site-binding ligand-based gene analysis suitable for the practical use.…”

Section: Introductionmentioning

confidence: 99%

Competitive Binding of Abasic Site-Binding Ligands and Masking Ligands to DNA Duplexes for the Analysis of Single-Base Mutation

et al. 2013

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We describe a competitive binding assay for the analysis of single-base mutation by using abasic site (AP site)-specific binding fluorescent ligands and masking ligands bound to the AP site in DNA duplexes. 2-Amino-5,6,7-trimethyl-1,8-naphthyridine (ATMND) can strongly bind to not only cytosine (C), but also thymine (T) opposite an AP site in the DNA duplexes (K11/10 7 M -1 : C, 15; T, 7.0). By contrast, in the presence of lumichrome (Lch) as a masking ligand, ATMND shows a clear binding selectivity for C over T (K11/10 7 M -1 : C, 7.0; T, 0.57), which is ascribed to the effective masking effect of Lch to the ATMND-T interaction in the AP site-containing DNA duplexes. It was shown that the competitive binding of ATMND and Lch to the AP site allowed the highly selective detection of C-related single-base mutation in DNAs amplified by polymerase chain reaction.

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“…24,25 Furthermore, an aqueous LC solution exhibits a single fluorescence band at 479 nm with the lifetime of 2.7 ns. 26 On the other hand, RFH2 is produced by photochemical protonation of the N(1) and N(5) atoms in RF and subsequent rearrangements of the double bonds of the ring structure, as illustrated in Fig. 1.…”

Section: Effects Of Acetic Acid On Tir Fluorescence Spectra Of Rf At mentioning

confidence: 99%

Photoinduced Redox Cycle of Riboflavin at a Water/Oil Interface

Ishizaka

Kitamura

2004

ANAL. SCI.

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IntroductionPhot proteins were found recently to be blue-light receptors in plants and fungi, which played essential roles in phototropic plant movements and chloroplast relocation. [1][2][3][4] All of the phot proteins contain two LOV (light-, oxygen-, and voltagesensitive) domains that consist of approximately 100 aminoacid residues. Each LOV domain binds a single flavin mononucleotide molecule (FMN in Fig. 1) through noncovalent interactions such as hydrogen-bonding, π-π stacking, and electrostatic interactions. 5,6 It is believed that formation of a cysteine-adduct of FMN is the signaling state of the protein. One proposed reaction scheme for this protein signaling is a reversible photoinduced redox cycle of FMN; absorption of near-UV -blue light by oxidized flavin (Fl) produces dihydroflavin (FlH2) through a flavosemiquinon radical intermediate (FlH·), which is oxidized subsequently to Fl by molecular oxygen. 8 During the photocycle, the thiol group in cysteine composed of the protein reacts with the 4α-position of FMN, giving rise to formation of the cysteine-FMN adduct. On the other hand, Scuttrigkeit et al. have reported that the cysteine-FMN adduct is produced from the excited triplet-state of FMN, since the excited singlet-triplet intersystem crossing rate and the excited triplet-state yield of FMN in the wild-type LOV2 domain are larger than those of FMN in solution. 9 According to the X-ray structural analysis of the LOV2 domain isolated from Adiantum capillus-veneris, furthermore, FMN is bound with the interior of the protein through hydrogen-bonding networks, and such a flavin-binding pocket in the protein posesses two water molecules. 6 Therefore, such a noncovalent interaction would also influence the reactivity of the groundand/or excited-states of FMN.FMN also catalyzes various biological one-and two-electron redox reactions in the dark. The noncovalent interactions such as hydrogen-bonding, π-π stacking, and electrostatic interactions within the enzyme have been reported to play essential roles in tuning the redox properties of FMN and, thus, in controlling the overall catalytic activity of the enzyme.10 On the basis of cyclic voltammetry, in practice, Rotello and coworkers have reported that 10-isobuthyl-flavin in dichloromethane, bound with an artificial receptor through triple hydrogen-bonds, shows a reduction potential value 100 mV A photoinduced redox reaction cycle of Riboflavin (RF) at a water/CCl4 interface was studied directly by means of both steady-state and time-resolved total internal reflection (TIR) fluorescence spectroscopies. The TIR fluorescence spectrum of RF observed at the water/CCl4 interface with the maximum wavelength of 517 nm was assigned to the π-π* transition from the excited singlet-state of the isoalloxazine chromophore in RF. Upon prolonged laser irradiation (400 nm) in the presence of N, N-dioctadecyl-[1,3,5]triazine-2,4,6-triamine (DTT) as a guest for RF in the CCl4 phase, on the other hand, a new TIR fluorescence band appeared at around 480 nm. Furthermore, th...

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Spectroscopy and Photophysics of Lumiflavins and Lumichromes

Cited by 131 publications

References 39 publications

Theoretical study of the electronic spectra of oxidized and reduced states of lumiflavin and its derivative

Theoretical study of the electronic spectra of oxidized and reduced states of lumiflavin and its derivative

Competitive Binding of Abasic Site-Binding Ligands and Masking Ligands to DNA Duplexes for the Analysis of Single-Base Mutation

Photoinduced Redox Cycle of Riboflavin at a Water/Oil Interface

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