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Luminescence emission spectra

Figure 12.2 Effect of the addition of 0.65 mg L 1 cyanide on the luminescence emission spectra of surface-modified CdSe QDs. Figure 12.2 Effect of the addition of 0.65 mg L 1 cyanide on the luminescence emission spectra of surface-modified CdSe QDs.
Experimental data on luminescent emission spectra are usually presented as relative emitted energy per constant wavelength interval, i.e. 4>a vs A. Usually the maximum of this curve is considered to be the peak of the emission band. [Pg.225]

FIGURE 16.5 Luminescence emission spectra and pictures from SWCNTs dispersed with the aid of polyimide in DMF (left) and the PI-NHj-SWCNT in DMF solution (right). The nanotube and polymer contents in the two samples were comparable. (Adapted from Lin, Y. et al., 7. Phys. Chem. B, 109, 14779, 2005.)... [Pg.470]

Figure 8.14 Luminescence emission spectra (excitation at 579.36nm) of Eu(STHP) in 20mM HEPES, lOOmM NaCI upon addition of phosphate (0-20mM), at pH 7.2, with WOfiM Eu(STHP). Addition of phosphate leads to a decrease in the emission peak at 592 nm ( Dg - F ), a decrease in the major emission peak at 614nm ( Dg - 62), and a decrease in the major emission band at 680nm ( Dg Reproduced with permission from [8],... Figure 8.14 Luminescence emission spectra (excitation at 579.36nm) of Eu(STHP) in 20mM HEPES, lOOmM NaCI upon addition of phosphate (0-20mM), at pH 7.2, with WOfiM Eu(STHP). Addition of phosphate leads to a decrease in the emission peak at 592 nm ( Dg - F ), a decrease in the major emission peak at 614nm ( Dg - 62), and a decrease in the major emission band at 680nm ( Dg Reproduced with permission from [8],...
Luminescence of Pyrosoma. All species of the genus Pyrosoma (about 10 species) are bioluminescent. Pyrosoma is one of the few organisms reported to luminesce in response to light (Bowlby et al., 1990). The luminescence emission spectrum of Pyrosoma atlantica is bimodal according to Kampa and Boden (1957), with the primary peak near 482 nm, and the secondary near 525 nm. Swift et al. (1977) reported the emission maxima of two Pyrosoma species at 485 and 493 nm, respectively, and Bowlby et al. (1990) found an emission peak at 475 nm with P. atlantica. A corrected bioluminescence spectrum of P. atlantica (A.max 485 nm) reported by Herring (1983) is shown in Fig. 10.5.2. [Pg.320]

The luminescence emission spectrum of a specimen is a plot of luminescence intensity, measured in relative numbers of quanta per unit frequency interval, against frequency. When the luminescence monochromator is scanned at constant slit width and constant amplifier sensitivity, the curve obtained is the apparent emission spectrum. To determine the true spectrum the apparent curve has to be corrected for changes of the sensitivity of the photomultiplier, the bandwidth of the monochromator, and the transmission of the monochromator with fre-... [Pg.314]

There is good evidence from 13C NMR and electronic spectra for an enzyme-bound reduced flavin hydroperoxide as in Eq. 15-31. While this hydroperoxide can decompose slowly to flavin and H202 in the dark, it can also carry out the oxidation of the aldehyde with emission of light.685/685a The luminescent emission spectrum resembles the fluorescence spectrum of the 4a -OH adduct (Eq. 23-49), which is probably the light-emitting species.686-688... [Pg.1346]

Note that this reasoning on the dependence of parameter A on the location depth of the recombination site has only a qualitative character. The actual samples of CdS have always a particle size distribution. Both the quencher adsorption constant and the luminescence emission spectrum depend on the particle size. This introduces a certain error into the A value obtained from fitting by the Eq. (2.19). The error should be particularly great for the deep and shallow energy levels of the surface recombination site. [Pg.59]

It will be noted experimentally that the peak wavelength in the luminescence emission spectrum is typically about 4-5 nm larger than that for the n = 1 exciton absorption peak. This Stokes shift is generally attributed to the spin fine stracture of exciton states similar but generally smaller Stokes shifts are seen in molecular electronic spectra. [Pg.495]

Fig. 1.5 Fluorescence emission spectrum of the luciferase-oxyluciferin complex in the same solution as in Fig. 1.4 (solid line), compared with the luminescence spectrum of firefly luciferin measured in glycylglycine buffer, pH 7.6 (dotted line). The former curve from Gates and DeLuca, 1975 the latter from Selinger and McElroy, 1960, both with permission from Elsevier. Fig. 1.5 Fluorescence emission spectrum of the luciferase-oxyluciferin complex in the same solution as in Fig. 1.4 (solid line), compared with the luminescence spectrum of firefly luciferin measured in glycylglycine buffer, pH 7.6 (dotted line). The former curve from Gates and DeLuca, 1975 the latter from Selinger and McElroy, 1960, both with permission from Elsevier.
Fig. 4.1.3 Absorption spectra of aequorin (A), spent solution of aequorin after Ca2+-triggered luminescence (B), and the chromophore of aequorin (C). Fluorescence emission spectrum of the spent solution of aequorin after Ca2+-triggered bioluminescence, excited at 340 nm (D). Luminescence spectrum of aequorin triggered with Ca2+ (E). Curve C is a differential spectrum between aequorin and the protein residue (Shimomura et al., 1974b) protein concentration 0.5 mg/ml for A and B, 1.0 mg/ml for C. From Shimomura and Johnson, 1976. Fig. 4.1.3 Absorption spectra of aequorin (A), spent solution of aequorin after Ca2+-triggered luminescence (B), and the chromophore of aequorin (C). Fluorescence emission spectrum of the spent solution of aequorin after Ca2+-triggered bioluminescence, excited at 340 nm (D). Luminescence spectrum of aequorin triggered with Ca2+ (E). Curve C is a differential spectrum between aequorin and the protein residue (Shimomura et al., 1974b) protein concentration 0.5 mg/ml for A and B, 1.0 mg/ml for C. From Shimomura and Johnson, 1976.
Fig. 4.2.2 Left panel-. Uncorrected Ca2+-triggered bioluminescence spectrum of W92F obelin derived from O. longissima. Right panel Corrected bioluminescence spectrum of the same obelin (dotted line), and the fluorescence emission spectrum of the spent solution after luminescence (solid line). From Deng et al., 2001, with permission of the Federation of the European Biochemical Societies. Fig. 4.2.2 Left panel-. Uncorrected Ca2+-triggered bioluminescence spectrum of W92F obelin derived from O. longissima. Right panel Corrected bioluminescence spectrum of the same obelin (dotted line), and the fluorescence emission spectrum of the spent solution after luminescence (solid line). From Deng et al., 2001, with permission of the Federation of the European Biochemical Societies.
Fig. 7.1.5 Fluorescence spectra of purified Chaetopterus photoprotein (CPA) in 10 mM ammonium acetate, pH 6.7 (solid lines), and the bioluminescence spectrum of the luminous slime of Chaetopterus in 10 mM Tris-HCl, pH 7.2 (dashed line). Note that the luminescence spectrum of Chaetopterus photoprotein in 2 ml of 10 mM Tris-HCl, pH 7.2, containing 0.5 M NaCl, 5 pi of old dioxane and 2 pi of 10 mM FeSC>4 (Amax 453-455 nm) matched exactly with the fluorescence emission spectrum of the photoprotein. No significant change was observed in the fluorescence spectrum after the luminescence reaction. Fig. 7.1.5 Fluorescence spectra of purified Chaetopterus photoprotein (CPA) in 10 mM ammonium acetate, pH 6.7 (solid lines), and the bioluminescence spectrum of the luminous slime of Chaetopterus in 10 mM Tris-HCl, pH 7.2 (dashed line). Note that the luminescence spectrum of Chaetopterus photoprotein in 2 ml of 10 mM Tris-HCl, pH 7.2, containing 0.5 M NaCl, 5 pi of old dioxane and 2 pi of 10 mM FeSC>4 (Amax 453-455 nm) matched exactly with the fluorescence emission spectrum of the photoprotein. No significant change was observed in the fluorescence spectrum after the luminescence reaction.
In the presence of an alkali salt, strong metal atom emission can be seen both in the emission spectrum and visually. This form of emission is described in detail in Chapter 13. Long-time exposure photographs comparing sonoluminescence and luminol and Na sonochemical luminescence are shown in Fig. 15.5a-c. [Pg.394]

Photophysical Processes in Pol,y(ethy1eneterephthalate-co-4,4 -biphenyldicarboxyl ate) (PET-co-4,4 -BPDC). The absorption and luminescence properties of PET are summarized above. At room temperature the absorption spectrum of PET-co-4,4 -BPDC copolymers, with concentrations of 4,4 -BPDC ranging from 0.5 -5.0 mole percent, showed UV absorption spectra similar to that of PET in HFIP. The corrected fluorescence spectra of the copolymers in HFIP exhibited excitation maxima at 255 and 290 nm. The emission spectrum displayed emission from the terephthalate portion of the polymer, when excited by 255 nm radiation, and emission from the 4,4 -biphenyldicarboxylate portion of the polymer when excited with 290 nm radiation. [Pg.248]

TGA, iodometric, mid-IR, luminescence (fluorescence and phosphorescence) and colour formation (yellowness index according to standard method ASTM 1925) were all employed in a study of aspects of the thermal degradation of EVA copolymers [67], Figure 23 compares a set of spectra from the luminescence analysis reported in this work. In the initial spectra (Figure 23(a)) of the EVA copolymer, two excitation maxima at 237 and 283 nm are observed, which both give rise to one emission spectrum with a maximum at 366 nm weak shoulders... [Pg.419]

More fluorescence features than just the emission intensity can be used to develop luminescent optosensors with enhanced selectivity and longer operational lifetime. The wavelength dependence of the luminescence (emission spectmm) and of the luminophore absorption (excitation spectrum) is a source of specificity. For instance, the excitation-emission matrix has shown to be a powerful tool to analyze complex mixtures of fluorescent species and fiber-optic devices for in-situ measurements (e.g. [Pg.105]

Different lanthanide metals also produce different emission spectrums and different intensities of luminescence at their emission maximums. Therefore, the relative sensitivity of time-resolved fluorescence also is dependent on the particular lanthanide element complexed in the chelate. The most popular metals along with the order of brightness for lanthanide chelate fluorescence are europium(III) > terbium(III) > samarium(III) > dysprosium(III). For instance, Huhtinen et al. (2005) found that lanthanide chelate nanoparticles used in the detection of human prostate antigen produced relative signals for detection using europium, terbium, samarium, and dysprosium of approximately 1.0 0.67 0.16 0.01, respectively. The emission... [Pg.476]

Because of the high sensitivity of Ti-containing luminescence centers to their local environments, photoluminescence spectroscopy can be applied to discriminate between various kinds of tetrahedral or near-tetrahedral titanium sites, such as perfectly closed Ti(OSi)4 and defective open Ti(OSi)3(OH) units. Lamberti et al. (49) reported an emission spectrum of TS-1 with a dominant band at 495 nm, with a shoulder at 430 nm when the sample was excited at 250 nm. When the excitation wavelength was 300 nm, the emission spectrum was characterized by a dominant band at 430 nm with a shoulder at 495 nm. These spectra and their dependence on the excitation wavelength clearly indicate the presence of two slightly different families of luminescent Ti species, which differ in their local environments, in agreement with EXAFS measurements carried out on the same samples. [Pg.37]


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Luminescence emission

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Luminescent emissions

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Spectra luminescent

Spectrum emission

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