Structure and Dynamics of Macromolecules: Absorption and Fluorescence Studies 2004
DOI: 10.1016/b978-044451449-3/50003-4
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Fluorophores: Descriptions and Properties

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Cited by 9 publications
(11 citation statements)
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“…Galbán et al [26] reported the average fluorescence lifetime of riboflavin to be 5.06 ns, FMN 4.7 to be ns, and FAD to be 2.27 ns. This is supported by Albani, who stated that τ FAD = 2.3 ns and τ FMN = 4.7 ns [27]. Although we did not get the same discernment in this particular experiment, we do strongly agree with these values because of the average fluorescence lifetimes we concluded to be connected with flavins in the cells (see Section 3.3).…”
Section: Analysis Of Emission Spectra Of Flavins and Whole Bacterial ...supporting
confidence: 84%
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“…Galbán et al [26] reported the average fluorescence lifetime of riboflavin to be 5.06 ns, FMN 4.7 to be ns, and FAD to be 2.27 ns. This is supported by Albani, who stated that τ FAD = 2.3 ns and τ FMN = 4.7 ns [27]. Although we did not get the same discernment in this particular experiment, we do strongly agree with these values because of the average fluorescence lifetimes we concluded to be connected with flavins in the cells (see Section 3.3).…”
Section: Analysis Of Emission Spectra Of Flavins and Whole Bacterial ...supporting
confidence: 84%
“…As was written in Section 3.1, one team led by Galbán [26] reported the average fluorescence lifetime of riboflavin to be 5.06 ns, FMN to be 4.7 ns, and FAD to be 2.27 ns. The second team, led by Albani, supported these values, and their experiments yielded values of τFAD = 2.3 ns and τFMN = 4.7 ns [27]. We strongly agree with these values because of the average fluorescence lifetimes we concluded to be connected with flavins in the cells (see Section 3.3).…”
Section: Analysis Of Emission Spectra Of Flavins and Whole Bacterial ...supporting
confidence: 71%
“…The lectin did not show autofluorescence, since lectins that present saccharides are non-fluorescent molecules [59]. On the other hand, the analysis of the QD alone showed one peak of fluorescence spectral emission at 570 nm.…”
Section: Discussionmentioning
confidence: 89%
“…However, porphyrins like heme precursors and other derivatives do possess inherent fluorescence when lacking the quenching iron atoms, typically exhibiting emission peaks in the 620-635 nm range when excited at 405 nm (Fauaz et al, 2010) (Figure 2c,d). This porphyrin fluorescence is especially notable when the Wetlaufer, 1963), (b) Emission spectra (redrawn from Albani, 2004) of aromatic amino acids tryptophan, tyrosine, and phenylaniline. (c) Excitation spectra and (d) emission spectra of collagen (black), elastin (blue), porphyrins (red), lipo-pigments (cyan) and pyridoxine (green) (redrawn from Wagnieres et al, 1998).…”
Section: Different Components Of the Blood And Their Source Of Autofl...mentioning
confidence: 99%
“…Absorption, emission, and excitation spectra endogenous fluorophores. (a) Absorption (redrawn from Wetlaufer, 1963), (b) Emission spectra (redrawn from Albani, 2004) of aromatic amino acids tryptophan, tyrosine, and phenylaniline. (c) Excitation spectra and (d) emission spectra of collagen (black), elastin (blue), porphyrins (red), lipo‐pigments (cyan) and pyridoxine (green) (redrawn from Wagnieres et al, 1998).…”
Section: Source Of Autofluorescence Of Bloodmentioning
confidence: 99%