Power-Law Kinetics in the Photoluminescence of Dye-Sensitized Nanoparticle Films: Implications for Electron Injection and Charge Transport

2012 ◽  
Vol 116 (30) ◽  
pp. 15888-15899 ◽  
Author(s):  
Ian J. McNeil ◽  
Dennis L. Ashford ◽  
Hanlin Luo ◽  
Christopher J. Fecko
2007 ◽  
Vol 111 (2) ◽  
pp. 1035-1041 ◽  
Author(s):  
María Quintana ◽  
Tomas Edvinsson ◽  
Anders Hagfeldt ◽  
Gerrit Boschloo

2019 ◽  
Vol 233 (9) ◽  
pp. 1247-1259
Author(s):  
Madhu Prakasam

Abstract In this work, we systematically investigate the impacts of electron-donor based on Triphenylamine (TPA). The Geometry structure, energy levels, light-harvesting ability and ultraviolet-visible absorption spectra were calculated by using Density Functional Theory (DFT) and Time-Dependent-DFT. The electron injection rate of the TPA-N(CH3)2 based dyes has 0.71 eV for high among the dye sensitizer. The First and Second order Hyperpolarizability of the 11.95 × 10−30 e.s.u and 12195.54 a.u, respectively for TPA-N(CH3)2 based dye. The calculated absorption spectra were showed in the ultra-violet visible region for power conversion region. The study reveals that the electron transfer character of TPA-N(CH3)2 based dyes can be made suitable for applications in Dye-Sensitized Solar Cells.


2018 ◽  
Vol 115 (3) ◽  
pp. 513-518 ◽  
Author(s):  
Iris Grossman-Haham ◽  
Gabriel Rosenblum ◽  
Trishool Namani ◽  
Hagen Hofmann

Protein dynamics are typically captured well by rate equations that predict exponential decays for two-state reactions. Here, we describe a remarkable exception. The electron-transfer enzyme quiescin sulfhydryl oxidase (QSOX), a natural fusion of two functionally distinct domains, switches between open- and closed-domain arrangements with apparent power-law kinetics. Using single-molecule FRET experiments on time scales from nanoseconds to milliseconds, we show that the unusual open-close kinetics results from slow sampling of an ensemble of disordered domain orientations. While substrate accelerates the kinetics, thus suggesting a substrate-induced switch to an alternative free energy landscape of the enzyme, the power-law behavior is also preserved upon electron load. Our results show that the slow sampling of open conformers is caused by a variety of interdomain interactions that imply a rugged free energy landscape, thus providing a generic mechanism for dynamic disorder in multidomain enzymes.


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