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Phosphorescence Quenching (phosphorescence + quenching)
Selected AbstractsDiffusion and Monod kinetics to determine in vivo human corneal oxygen-consumption rate during soft contact-lens wearJOURNAL OF BIOMEDICAL MATERIALS RESEARCH, Issue 1 2009Mahendra Chhabra Abstract The rate of oxygen consumption is an important parameter to assess the physiology of the human cornea. Metabolism of oxygen in the cornea is influenced by contact-lens-induced hypoxia, diseases such as diabetes, surgery, and drug treatment. Therefore, estimation of in vivo corneal oxygen-consumption rate is essential for gauging adequate oxygen supply to the cornea. Phosphorescence quenching of a dye coated on the posterior of a soft contact lens provides a powerful technique to measure tear-film oxygen tension (Harvitt and Bonanno, Invest Ophthalmol Vis Sci 1996;37:1026,1036; Bonanno et al., Invest Ophthalmol Vis Sci 2002;43:371,376). Unfortunately, previous work in establishing oxygen-consumption kinetics from transient postlens tear-film oxygen tensions relies on the simplistic assumption of a constant corneal-consumption rate. A more realistic model of corneal metabolism is needed to obtain reliable oxygen-consumption kinetics. Here, physiologically relevant nonlinear Monod kinetics is adopted for describing the local oxygen-consumption rate, thus avoiding aphysical negative oxygen tensions in the cornea. We incorporate Monod kinetics in an unsteady-state reactive-diffusion model for the cornea contact-lens system to determine tear-film oxygen tension as a function of time when changing from closed-eye to open-eye condition. The model was fit to available experimental data of in vivo human postlens tear-film oxygen tension to determine the corneal oxygen-consumption rate. Reliance on corneal oxygen diffusivity and solubility data obtained from rabbits is no longer requisite. Excellent agreement is obtained between the proposed model and experiment. We calculate the spatial-averaged in vivo human maximum corneal oxygen-consumption rate as Q = 1.05 × 10,4 mL/(cm3 s). The calculated Monod constant is Km = 2.2 mmHg. © 2008 Wiley Periodicals, Inc. J Biomed Mater Res Part B: Appl Biomater, 2009 [source] Design and Synthesis of Phosphorescent Iridium Containing Dendrimers for Potential Applications in Organic Light-Emitting Diodes,MACROMOLECULAR CHEMISTRY AND PHYSICS, Issue 18 2008Qin-De Liu Abstract Three phosphorescent dendrimers (IrC1, IrC3, and IrF2) with an iridium complex core and oligocarbazole or oligofluorene substituted ligands were synthesized and characterized. The structures of the oligocarbazole were designed to maintain high triplet energy of the ligands so that phosphorescence quenching in the resulting dendrimers can be prevented, while the oligofluorene in IrF2 resulted in undesired phosphorescence quenching. Best performance was obtained from an IrC3 based electrophosphorescent light-emitting device with a maximum luminance of 13,060 cd,·,m,2 at a driving voltage of 11.5 V and a peak current-efficiency of 4.3 cd,·,A,1 at a luminance of 3,400 cd,·,m,2, owing to its high PL efficiency, and efficient energy transfer between the iridium complex core and the ligands. [source] Simple determination of the herbicide napropamide in water and soil samples by room temperature phosphorescencePEST MANAGEMENT SCIENCE (FORMERLY: PESTICIDE SCIENCE), Issue 8 2005Alfonso Salinas-Castillo Abstract A new, simple, rapid and selective phosphorimetric method for determining napropamide is proposed which demonstrates the applicability of heavy-atom-induced room-temperature phosphorescence for analyzing pesticides in real samples. The phosphorescence signals are a consequence of intermolecular protection and are found exclusively with analytes in the presence of heavy atom salts. Sodium sulfite was used as an oxygen scavenger to minimize room-temperature phosphorescence quenching. The determination was performed in 1 M potassium iodide and 6 mM sodium sulfite at 20 °C. The phosphorescence intensity was measured at 520 nm with excitation at 290 nm. Phosphorescence was easily developed, with a linear relation to concentration between 3.2 and 600.0 ng ml,1 and a detection limit of 3.2 ng ml,1. The method has been successfully applied to the analysis of napropamide in water and soil samples and an exhaustive interference study was also carried out to display the selectivity of the proposed method. Copyright © 2005 Society of Chemical Industry [source] Flexibility in Proteins: Tuning the Sensitivity to O2 Diffusion by Varying the Lifetime of a Phosphorescent Sensor in Horseradish Peroxidase,PHOTOCHEMISTRY & PHOTOBIOLOGY, Issue 1 2004Janna Nibbs ABSTRACT The heme in horseradish peroxidase (HRP) was replaced by phosphorescent Pt-mesoporphyrin IX (PtMP), which acted as a phosphorescent marker of oxygen quenching and allowed comparison with another probe, Pd-mesoporphyrin IX (Khajehpour et al. (2003) Proteins 53, 656,666). Benzohydroxamic acid (BHA), a competitive inhibitor of the enzyme, was also used to monitor its effects on phosphorescence quenching. With the addition of BHA, in the presence of oxygen, the phosphorescence intensity of the protein increased. In contrast, the addition of BHA, in the absence of oxygen, reduced the phosphorescence intensity of the protein. Kd= 18 ,M when BHA binds to PtMP-HRP. The effect of BHA can be explained by two factors: (1) BHA reduces the accessibility of O2 to the protein interior and (2) BHA itself quenches the phosphorescence. Consistent with this, the oxygen quenching of the phosphorescence of PtMP-HRP gave a quenching constant of kq= 234 mm Hg,1 s,1 in the absence of BHA and kq= 28.7 mm Hg,1 s,1 in the presence of BHA. The quenching rate of BHA is 4000 s,1. The relative quantum yield of the phosphorescence of the Pt derivative is about six times that of the Pd derivative, whereas the phosphorescence lifetime is approximately eight times shorter. The high quantum yield and suitable lifetime make Pt-porphyrins appropriate as sensors of O2 diffusion and flexibility in heme proteins. [source] | ||||||||||