Phosphorescence lifetimes for

The phosphorescence lifetimes for the p-aminobenzoic acid anion adsorbed on sodium acetate as a function of temperature were evaluated in a manner similar to the one discussed by Oelkrug and coworkers (,28-30) for polycyclic aromatic hydrocarbons adsorbed on y-alumina. In general, the solid-surface phosphorescence lifetime cutrves for the anion of p-aminobenzoic acid followed Equation 2. 

Burrell and Hurtubise (.32) investigated calibration curves extended well beyond the normal linear range for RTF and RTF of benzoCf)quino-line adsorbed on a silica gel chromatoplate under neutral and acidic conditions. As the benzoCf)quinoline concentration increased, the RTF curves leveled off, whereas the RTF curves passed through a maximum and then decreased. The extended calibration curves along with fluorescence and phosphorescence spectra and phosphorescence lifetimes for benzoCf)quinoline revealed differences in the RTF and RTF phenomena. For example, it was determined that RTF could arise from molecules adsorbed on the surface and in multilayers of molecules, whereas phosphorescence was only generated from molecules adsorbed on the surface of the chromatoplate and not in the multilayers. ... 

Kiittner et al. also determined the phosphorescence lifetimes for both isotopic species by excitation of the vibrationless level of the singlet state of pressures above 0.5 torr to exclude effects due to wall quenching. By application of a magnetic field they found the phosphorescence lifetime to be unaffected. From the Stern-Volmer plots, the zero pressure lifetimes are found to be 3.3 msec for glyoxal-/i and 6.1 msec for glyoxal-d, which are in agreement with the values reported by Yardley (1972). 

Molecular Phosphorescence Instrumentation for molecular phosphorescence must discriminate between phosphorescence and fluorescence. Since the lifetime for fluorescence is much shorter than that for phosphorescence, discrimination is easily achieved by incorporating a delay between exciting and measuring phosphorescent emission. A typical instrumental design is shown in Figure 10.46. As shown... 

Emission of light due to an allowed electronic transition between excited and ground states having the same spin multiplicity, usually singlet. Lifetimes for such transitions are typically around 10 s. Originally it was believed that the onset of fluorescence was instantaneous (within 10 to lO-" s) with the onset of radiation but the discovery of delayed fluorescence (16), which arises from thermal excitation from the lowest triplet state to the first excited singlet state and has a lifetime comparable to that for phosphorescence, makes this an invalid criterion. Specialized terms such as photoluminescence, cathodoluminescence, anodoluminescence, radioluminescence, and Xray fluorescence sometimes are used to indicate the type of exciting radiation. 

Solid-surface room-temperature phosphorescence (RTF) is a relatively new technique which has been used for organic trace analysis in several fields. However, the fundamental interactions needed for RTF are only partly understood. To clarify some of the interactions required for strong RTF, organic compounds adsorbed on several surfaces are being studied. Fluorescence quantum yield values, phosphorescence quantum yield values, and phosphorescence lifetime values were obtained for model compounds adsorbed on sodiiun acetate-sodium chloride mixtures and on a-cyclodextrin-sodium chloride mixtures. With the data obtained, the triplet formation efficiency and some of the rate constants related to the luminescence processes were calculated. This information clarified several of the interactions responsible for RTF from organic compounds adsorbed on sodium acetate-sodium chloride and a-cyclodextrin-sodium chloride mixtures. Work with silica gel chromatoplates has involved studying the effects of moisture, gases, and various solvents on the fluorescence and phosphorescence intensities. The net result of the study has been to improve the experimental conditions for enhanced sensitivity and selectivity in solid-surface luminescence analysis. 

Solid-surface fluorescence and phosphorescence quantum yield values were obtained from +23° to -180°C for the anion of p-aminobenzoic acid adsorbed on sodium acetate (11). Fhosphorescence lifetime values were also obtained for the adsorbed anion from +23° to -196°C. Table 1 gives the fluorescence and phosphorescence quantum yield values acquired. The fluorescence quantum yield values remained practically constant as a function of temperature. However, the phosphorescence quantum yield values changed substantially with temperature. The phosphorescence lifetime experiments indicated two decaying components. Each component showed a gradual increase in phosphorescence lifetime with cooler temperatures, but then the increase appeared to level off at the coldest temperatures. 

Sodium Acetate-Sodium Chloride Mixtures. Ramasamy and Hurtubise (12) obtained RTF and RTF quantum yields, triplet formation efficiency, and phosphorescence lifetime values for the anion of p-aminobenzoic acid adsorbed on sodium acetate and on several sodium acetate-sodium chloride mixtures. Rate constants were calculated for phosphorescence and for radiationless transition from the triplet state. The results showed that several factors were important for maximum RTF from the anion of p-aminobenzoic acid. One of the most important of these was how efficiently the matrix was packed with sodium acetate molecules. A similar conclusion was found for RTF however, the RTF quantum yield increased more dramatically than the RTF quantum yield. 

The absorption bands measured by the flash spectrographic method are often assigned by (a) comparison with known singlet-singlet absorption spectra, (b) comparison of the lifetime of the species responsible for the absorption with the phosphorescence lifetime, (c) comparison with calculated energies and intensities of the various possible absorptions by semi-empirical molecular orbital methods, and (d) comparison with published triplet absorption spectra and decay kinetics of model compounds. 

Other work by Tsuboyama et al. reported a very highly efficient red PHOLED with power efficiency of 8.0 lm/W at 100 cd/m2 using Ir(piq)3 as a dopant [362], Most exciting, however, is the relatively recent demonstration of exceptional lifetimes for these materials in OLED devices where work from UDC has claimed a 14 cd/A red CIE (0.65, 0.35) with a lifetime of 25,000 h at 500 nit. Such performance promises much for phosphorescent red emitters in commercial devices and even higher efficiencies have been realized in systems that compromise the chromaticity toward the deep red with CIE (0.67, 0.33) and lifetimes >100,000 h at 500 cd/m2 [363],... 

Another efficient material introduced by the same group is the green emitting /ac-tris(2-phenylpyridine)iridium [Ir(ppy)3, 67] [38], A suitable host for this phosphorescent emitter is CBP (10). The triplet lifetime is rather short, the experimentally determined value being 500 ns in the CBP matrix. Another iridium complex was shown to emit in the red with high efficiency due to the short phosphorescence lifetime in comparison with PtOEP [165]. 

Making the assumption that the rate of intersystem crossing is fast relative to phosphorescence emission, the decay of phosphorescence will be exponential and the observed lifetime for phosphorescence, for most conditions, will be governed only by three rates as given by Eq. (3.4) ... 

At 77 K the position of the 0-0 band is generally blue shifted for exposed tryptophans and red shifted for buried tryptophans. Along with a shift in wavelength to the red, the phosphorescence lifetime decreases.(28) The single tryptophan of human serum albumin shows red-shifted phosphorescence and D - L triplet zero-field splitting, indicating that it is in a hydrophobic environment. 29 ... 

The phosphorescence lifetimes of various proteins at room temperature are given in Table 3.1. Some variability in the lifetimes reported from lab to lab is evident, possibly due to different enzyme preparation, removal of oxygen (see below), or other conditions. Nevertheless, when measured under the same conditions, it is apparent that the tryptophan lifetimes vary dramatically from protein to protein. Alkaline phosphatase exhibits the longest lifetime from a protein in solution with a lifetime of 1.5—1.7 s at 22°C, approaching the lifetime of 5.5 s at 77 K. The lifetime of free indole in solution is 15—30 /is at 22°C.(38 39) Therefore, in the absence of other quenching mechanisms, the lower limit for the phosphorescence lifetime of a fully exposed tryptophan moiety in a protein should be about 20 /is. 

From an experimental viewpoint, the wide range of phosphorescence lifetimes is advantageous for the study of proteins. It means that it should be... 

It has been observed that for some proteins the room temperature phosphorescence lifetimes are increased in D20. The phosphorescence lifetime of liver alcohol dehydrogenase is 300 ms in H2Oand 500 ms in D2O.<10) Phosphorescence lifetimes are often dramatically increased by exchanging hydrogen with deuterium. The reason for this is that decay rates are affected by overtones of the C-H or N-H stretch. In the case of tryptophan in... 

For single-tryptophan proteins there is some correlation between blue-shifted fluorescence emission maximum and phosphorescence lifetime (Table 3.2). Another correlation is that three of the proteins which exhibit phosphorescence, azurin, protease (subtilisin Carlsberg), and ribonuclease Tlt are reported to show resolved fluorescence emission at 77 K. Both blue-shifted emission spectra and resolved spectra are characteristic of indole in a hydrocarbon-like matrix. 

Other groups within the protein may affect excited states. Disulfide bonds quench the excited states of tryptophan. For instance, at 77 K the phosphorescence lifetime of native lysozyme is low, 1.4s reduction of the disulfide bonds or denaturation gave the typical phosphorescence lifetime of 5.6 s.(49) Therefore, the absence of phosphorescence at room temperature from this protein is likely to be due to quenching of both the singlet and the triplet state. 

A survey of the quenching constants for a series of proteins was made using one quencher, nitrite (Table 3.4).(58) It is noted that the phosphorescence lifetime t0 is not correlated with the quenching constant. For example, the... 

The phosphorescence lifetimes have been examined for many protein systems as a function of temperature. In the early work oxygen was not removed from the sample.(72,73) In these works the lifetimes are dominated by quenching by oxygen, and so the temperature dependencies probably represent temperature-dependent oxygen diffusion. 

For horse liver alcohol dehydrogenase, denaturation by guanidine hydrochloride resulted in a decrease in phosphorescence lifetime parallel with loss of activity.(79) With urea as a denaturant, the decrease in phosphorescence lifetime appeared cooperative, and it is suggested that the denaturant loosened intramolecular interactions (such as hydrogen bonds), resulting in greater fluidity of the tryptophan environment.(80)... 

The various mechanisms which affect the Ti-<- Sq intensity and thus the radiative lifetime have been discussed earlier. For the class of aromatic hydrocarbons spin-orbit couphng is small and a t5q3ical value of about 30 sec for Tr seems appropriate However, the observed phosphorescence lifetimes vary greatly, demonstrating in most cases a dominating influence of the radiationless contribution. Siebrand and Williams > have noticed a very interesting correlation (Fig. 27) between the radiationless deactivation rate = 1 /rri and the triplet... 

At 77 K in EPA, lifetimes of 60 10 ms for 1-nitro- and 242 10 ms for 2-nitronaphthalene have been obtained from analysis of the transient absorption decay curves >. Differences to phosphorescence lifetimes under the same condi-... 

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