Physical mechanism of photoinduced intermolecular charge transfer enhanced by fluorescence resonance energy transfer

2018 ◽  
Vol 20 (19) ◽  
pp. 13558-13565 ◽  
Author(s):  
Huan Zong ◽  
Jiangcai Wang ◽  
Xijiao Mu ◽  
Xuefeng Xu ◽  
Jing Li ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Charge Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Physical Mechanism ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Intermolecular Charge Transfer ◽  
Donor Acceptor ◽  
Fluorescence Resonance

Photoinduced intermolecular charge transfer (PICT) and fluorescence resonance energy transfer (FRET) in donor–acceptor systems have been investigated experimentally and theoretically.

Control of Emission by Intermolecular Fluorescence Resonance Energy Transfer and Intermolecular Charge Transfer

2006 ◽  
Vol 110 (19) ◽  
pp. 6324-6328 ◽  
Author(s):  
Mengtao Sun ◽  
Tõnu Pullerits ◽  
Pär Kjellberg ◽  
Wichard J. D. Beenken ◽  
Keli Han
Keyword(s):  
Energy Transfer ◽  
Charge Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Intermolecular Charge Transfer ◽  
Fluorescence Resonance

Controlling fluorescence resonance energy transfer of donor–acceptor dyes by Diels–Alder dynamic covalent bonds

2021 ◽  
Vol 57 (26) ◽  
pp. 3275-3278
Author(s):  
Yanhui Cui ◽  
Fen Li ◽  
Xin Zhang
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Aromatic Amine ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Diels Alder ◽  
Covalent Bonds ◽  
Donor Acceptor ◽  
Fluorescence Resonance ◽  
Mutual Conversion

Two new dyes, consisting of an aromatic amine donor and dansyl acceptor connected by Diels–Alder bonds, display a switchable energy transfer. Dynamic covalent properties enable the mutual conversion of the two dyes by maleimide exchanges.

scholarly journals Cyan-emitting and orange-emitting fluorescent proteins as a donor/acceptor pair for fluorescence resonance energy transfer

2004 ◽  
Vol 381 (1) ◽  
pp. 307-312 ◽  
Author(s):  
Satoshi KARASAWA ◽  
Toshio ARAKI ◽  
Takeharu NAGAI ◽  
Hideaki MIZUNO ◽  
Atsushi MIYAWAKI
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Fluorescent Proteins ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Acceptor Pair ◽  
Donor And Acceptor ◽  
Donor Acceptor ◽  
Donor Acceptor Pair ◽  
Fluorescence Resonance

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.

scholarly journals Excitonic Heterodimer Formation in an HIV-1 Oligonucleotide Labeled with a Donor-Acceptor Pair Used for Fluorescence Resonance Energy Transfer

2003 ◽  
Vol 84 (1) ◽  
pp. 643-654 ◽  
Author(s):  
Serena Bernacchi ◽  
Etienne Piémont ◽  
Noelle Potier ◽  
Alain van Dorsselaer ◽  
Yves Mély
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Acceptor Pair ◽  
Donor Acceptor ◽  
Donor Acceptor Pair ◽  
Fluorescence Resonance ◽  
Hiv 1

scholarly journals Highly efficient fluorescence resonance energy transfer in co-encapsulated BODIPY nanoparticles

2021 ◽  
Vol 12 (4) ◽  
pp. 361-367
Author(s):  
Priyadarshine Hewavitharanage ◽  
Launa Steele ◽  
Isaac Dickenson
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Acceptor Pair ◽  
Highly Efficient ◽  
Fluorescence Measurements ◽  
Donor Acceptor ◽  
Donor Acceptor Pair ◽  
Fluorescence Resonance

Fluorescence resonance energy transfer (FRET) is a powerful tool used in a wide range of applications due to its high sensitivity and many other advantages. Co-encapsulation of a donor and an acceptor in nanoparticles is a useful strategy to bring the donor-acceptor pair in proximity for FRET. A highly efficient FRET system based on BODIPY-BODIPY (BODIPY:  boron-dipyrromethene) donor-acceptor pair in nanoparticles was synthesized. Nanoparticles were formed by co-encapsulating a green emitting BODIPY derivative (FRET donor, lmax = 501 nm) and a red emitting BODIPY derivative (FRET acceptor, lmax = 601 nm) in an amphiphilic polymer using the precipitation method. Fluorescence measurements of encapsulated BODIPY in water following 501 nm excitation caused a 3.6 fold enhancement of the acceptor BODIPY emission at 601 nm indicating efficient energy transfer between the green emitting donor BODIPY and the red emitting BODIPY acceptor with a 100 nm Stokes shift. The calculated FRET efficiency was 96.5%. Encapsulated BODIPY derivatives were highly stable under our experimental conditions.

Fluorescence resonance energy transfer between donor-acceptor pair on two oligonucleotides hybridized adjacently to DNA template

Biopolymers ◽  
2003 ◽  
Vol 72 (6) ◽  
pp. 401-412 ◽  
Author(s):  
L. Wang ◽  
A. K. Gaigalas ◽  
J. Blasic ◽  
M. J. Holden ◽  
D. T. Gallagher ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Acceptor Pair ◽  
Donor Acceptor ◽  
Donor Acceptor Pair ◽  
Fluorescence Resonance ◽  
Dna Template

scholarly journals Protein interaction quantified in vivo by spectrally resolved fluorescence resonance energy transfer

2004 ◽  
Vol 385 (1) ◽  
pp. 265-277 ◽  
Author(s):  
Valerică RAICU ◽  
David B. JANSMA ◽  
R. J. Dwayne MILLER ◽  
James D. FRIESEN
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Receptor Protein ◽  
Acceptor Pair ◽  
Donor Acceptor ◽  
Fret Efficiency ◽  
Fluorescence Resonance

We describe a fluorescence resonance energy transfer (FRET)-based method for finding in living cells the fraction of a protein population (αT) forming complexes, and the average number (n) of those protein molecules in each complex. The method relies both on sensitized acceptor emission and on donor de-quenching (by photobleaching of the acceptor molecules), coupled with full spectral analysis of the differential fluorescence signature, in order to quantify the donor/acceptor energy transfer. The approach and sensitivity limits are well suited for in vivo microscopic investigations. This is demonstrated using a scanning laser confocal microscope to study complex formation of the sterile 2 α-factor receptor protein (Ste2p), labelled with green, cyan, and yellow fluorescent proteins (GFP, CFP, and YFP respectively), in budding yeast Saccharomyces cerevisiae. A theoretical model is presented that relates the efficiency of energy transfer in protein populations (the apparent FRET efficiency, Eapp) to the energy transferred in a single donor/acceptor pair (E, the true FRET efficiency). We determined E by using a new method that relies on Eapp measurements for two donor/acceptor pairs, Ste2p–CFP/Ste2p–YFP and Ste2p–GFP/Ste2p–YFP. From Eapp and E we determined αT≈1 and n≈2 for Ste2 proteins. Since the Ste2p complexes are formed in the absence of the ligand in our experiments, we conclude that the α-factor pheromone is not necessary for dimerization.

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