ODMR investigation of the donor-acceptor pair orientation from triplet-triplet energy transfer within frozen SDS micelles

1986 ◽  
Vol 90 (8) ◽  
pp. 1643-1647 ◽  
Author(s):  
Sanjib Ghosh ◽  
Michael Petrin ◽  
August Maki
2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Runchen Lai ◽  
Yangyi Liu ◽  
Xiao Luo ◽  
Lan Chen ◽  
Yaoyao Han ◽  
...  

AbstractConventional wisdom posits that spin-triplet energy transfer (TET) is only operative over short distances because Dexter-type electronic coupling for TET rapidly decreases with increasing donor acceptor separation. While coherent mechanisms such as super-exchange can enhance the magnitude of electronic coupling, they are equally attenuated with distance. Here, we report endothermic charge-transfer-mediated TET as an alternative mechanism featuring shallow distance-dependence and experimentally demonstrated it using a linked nanocrystal-polyacene donor acceptor pair. Donor-acceptor electronic coupling is quantitatively controlled through wavefunction leakage out of the core/shell semiconductor nanocrystals, while the charge/energy transfer driving force is conserved. Attenuation of the TET rate as a function of shell thickness clearly follows the trend of hole probability density on nanocrystal surfaces rather than the product of electron and hole densities, consistent with endothermic hole-transfer-mediated TET. The shallow distance-dependence afforded by this mechanism enables efficient TET across distances well beyond the nominal range of Dexter or super-exchange paradigms.


2005 ◽  
Vol 11 (11) ◽  
pp. 3469-3481 ◽  
Author(s):  
Sébastien Faure ◽  
Christine Stern ◽  
Enrique Espinosa ◽  
Jasmin Douville ◽  
Roger Guilard ◽  
...  

2004 ◽  
Vol 381 (1) ◽  
pp. 307-312 ◽  
Author(s):  
Satoshi KARASAWA ◽  
Toshio ARAKI ◽  
Takeharu NAGAI ◽  
Hideaki MIZUNO ◽  
Atsushi MIYAWAKI

GFP (green fluorescent protein)-based FRET (fluorescence resonance energy transfer) technology has facilitated the exploration of the spatio-temporal patterns of cellular signalling. While most studies have used cyan- and yellow-emitting FPs (fluorescent proteins) as FRET donors and acceptors respectively, this pair of proteins suffers from problems of pH-sensitivity and bleeding between channels. In the present paper, we demonstrate the use of an alternative additional donor/acceptor pair. We have cloned two genes encoding FPs from stony corals. We isolated a cyan-emitting FP from Acropara sp., whose tentacles exhibit cyan coloration. Similar to GFP from Renilla reniformis, the cyan FP forms a tight dimeric complex. We also discovered an orange-emitting FP from Fungia concinna. As the orange FP exists in a complex oligomeric structure, we converted this protein into a monomeric form through the introduction of three amino acid substitutions, recently reported to be effective for converting DsRed into a monomer (Clontech). We used the cyan FP and monomeric orange FP as a donor/acceptor pair to monitor the activity of caspase 3 during apoptosis. Due to the close spectral overlap of the donor emission and acceptor absorption (a large Förster distance), substantial pH-resistance of the donor fluorescence quantum yield and the acceptor absorbance, as well as good separation of the donor and acceptor signals, the new pair can be used for more effective quantitative FRET imaging.


1999 ◽  
Vol 10 (6) ◽  
pp. 1107-1114 ◽  
Author(s):  
Uwe Schobel ◽  
Hans-Joachim Egelhaaf ◽  
Andreas Brecht ◽  
Dieter Oelkrug ◽  
Günter Gauglitz

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