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Förster Resonance Energy Transfer between Core/Shell Quantum Dots and Bacteriorhodopsin.

Griep MH, Winder EM, Lueking DR, Garrett GA, Karna SP, Friedrich CR - Mol Biol Int (2012)

Bottom Line: An energy transfer relationship between core-shell CdSe/ZnS quantum dots (QDs) and the optical protein bacteriorhodopsin (bR) is shown, demonstrating a distance-dependent energy transfer with 88.2% and 51.1% of the QD energy being transferred to the bR monomer at separation distances of 3.5 nm and 8.5 nm, respectively.Fluorescence lifetime measurements isolate nonradiative energy transfer, other than optical absorptive mechanisms, with the effective QD excited state lifetime reducing from 18.0 ns to 13.3 ns with bR integration, demonstrating the Förster resonance energy transfer contributes to 26.1% of the transferred QD energy at the 3.5 nm separation distance.The established direct energy transfer mechanism holds the potential to enhance the bR spectral range and sensitivity of energies that the protein can utilize, increasing its subsequent photocurrent generation, a significant potential expansion of the applicability of bR in solar cell, biosensing, biocomputing, optoelectronic, and imaging technologies.

View Article: PubMed Central - PubMed

Affiliation: Department of Mechanical Engineering Mechanics, Michigan Technological University, 815 RL Smith, 1400 Townsend Drive, Houghton, MI 49931, USA.

ABSTRACT
An energy transfer relationship between core-shell CdSe/ZnS quantum dots (QDs) and the optical protein bacteriorhodopsin (bR) is shown, demonstrating a distance-dependent energy transfer with 88.2% and 51.1% of the QD energy being transferred to the bR monomer at separation distances of 3.5 nm and 8.5 nm, respectively. Fluorescence lifetime measurements isolate nonradiative energy transfer, other than optical absorptive mechanisms, with the effective QD excited state lifetime reducing from 18.0 ns to 13.3 ns with bR integration, demonstrating the Förster resonance energy transfer contributes to 26.1% of the transferred QD energy at the 3.5 nm separation distance. The established direct energy transfer mechanism holds the potential to enhance the bR spectral range and sensitivity of energies that the protein can utilize, increasing its subsequent photocurrent generation, a significant potential expansion of the applicability of bR in solar cell, biosensing, biocomputing, optoelectronic, and imaging technologies.

No MeSH data available.


Related in: MedlinePlus

(a) Jablonski diagram showing FRET between a donor and an acceptor molecule. The purple arrow shows QD absorption, yellow arrow shows vibrational relaxation, and red solid arrow shows fluorescence. Solid blue arrow shows nonradiative energy transfer from the donor QD to acceptor biomolecule. (b) Theoretical FRET efficiency of a 565 nm emission QD (donor)-bR (acceptor) pair over a 0 nm–15 nm dipole separation range. The Förster radius of the QD-bR coupling system is calculated to be 7.94 nm.
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fig2: (a) Jablonski diagram showing FRET between a donor and an acceptor molecule. The purple arrow shows QD absorption, yellow arrow shows vibrational relaxation, and red solid arrow shows fluorescence. Solid blue arrow shows nonradiative energy transfer from the donor QD to acceptor biomolecule. (b) Theoretical FRET efficiency of a 565 nm emission QD (donor)-bR (acceptor) pair over a 0 nm–15 nm dipole separation range. The Förster radius of the QD-bR coupling system is calculated to be 7.94 nm.

Mentions: Using these equations, Ro is calculated to be 7.94 nm for a 565 nm QD/bR system and 7.76 nm for a 595 nm QD/bR system. Thus, with a separation of 7.94 nm between the QD and bR retinal molecule, half of the QD output energy should be transferred to the bR molecule nonphotonically through the energy transfer process depicted in Figure 2(a). The theoretical calculations also suggest that adjusting the QD emission peak from 565 nm to 595 nm only decreases Ro by 0.19 nm; therefore, the use of QDs with an emission peak directly at 570 nm is not critical. With the Förster radius values determined, the theoretical FRET efficiency (E) at varying QD-bR separation distances can be determined using (3) and is plotted in Figure 2(b):


Förster Resonance Energy Transfer between Core/Shell Quantum Dots and Bacteriorhodopsin.

Griep MH, Winder EM, Lueking DR, Garrett GA, Karna SP, Friedrich CR - Mol Biol Int (2012)

(a) Jablonski diagram showing FRET between a donor and an acceptor molecule. The purple arrow shows QD absorption, yellow arrow shows vibrational relaxation, and red solid arrow shows fluorescence. Solid blue arrow shows nonradiative energy transfer from the donor QD to acceptor biomolecule. (b) Theoretical FRET efficiency of a 565 nm emission QD (donor)-bR (acceptor) pair over a 0 nm–15 nm dipole separation range. The Förster radius of the QD-bR coupling system is calculated to be 7.94 nm.
© Copyright Policy - open-access
Related In: Results  -  Collection

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getmorefigures.php?uid=PMC3376779&req=5

fig2: (a) Jablonski diagram showing FRET between a donor and an acceptor molecule. The purple arrow shows QD absorption, yellow arrow shows vibrational relaxation, and red solid arrow shows fluorescence. Solid blue arrow shows nonradiative energy transfer from the donor QD to acceptor biomolecule. (b) Theoretical FRET efficiency of a 565 nm emission QD (donor)-bR (acceptor) pair over a 0 nm–15 nm dipole separation range. The Förster radius of the QD-bR coupling system is calculated to be 7.94 nm.
Mentions: Using these equations, Ro is calculated to be 7.94 nm for a 565 nm QD/bR system and 7.76 nm for a 595 nm QD/bR system. Thus, with a separation of 7.94 nm between the QD and bR retinal molecule, half of the QD output energy should be transferred to the bR molecule nonphotonically through the energy transfer process depicted in Figure 2(a). The theoretical calculations also suggest that adjusting the QD emission peak from 565 nm to 595 nm only decreases Ro by 0.19 nm; therefore, the use of QDs with an emission peak directly at 570 nm is not critical. With the Förster radius values determined, the theoretical FRET efficiency (E) at varying QD-bR separation distances can be determined using (3) and is plotted in Figure 2(b):

Bottom Line: An energy transfer relationship between core-shell CdSe/ZnS quantum dots (QDs) and the optical protein bacteriorhodopsin (bR) is shown, demonstrating a distance-dependent energy transfer with 88.2% and 51.1% of the QD energy being transferred to the bR monomer at separation distances of 3.5 nm and 8.5 nm, respectively.Fluorescence lifetime measurements isolate nonradiative energy transfer, other than optical absorptive mechanisms, with the effective QD excited state lifetime reducing from 18.0 ns to 13.3 ns with bR integration, demonstrating the Förster resonance energy transfer contributes to 26.1% of the transferred QD energy at the 3.5 nm separation distance.The established direct energy transfer mechanism holds the potential to enhance the bR spectral range and sensitivity of energies that the protein can utilize, increasing its subsequent photocurrent generation, a significant potential expansion of the applicability of bR in solar cell, biosensing, biocomputing, optoelectronic, and imaging technologies.

View Article: PubMed Central - PubMed

Affiliation: Department of Mechanical Engineering Mechanics, Michigan Technological University, 815 RL Smith, 1400 Townsend Drive, Houghton, MI 49931, USA.

ABSTRACT
An energy transfer relationship between core-shell CdSe/ZnS quantum dots (QDs) and the optical protein bacteriorhodopsin (bR) is shown, demonstrating a distance-dependent energy transfer with 88.2% and 51.1% of the QD energy being transferred to the bR monomer at separation distances of 3.5 nm and 8.5 nm, respectively. Fluorescence lifetime measurements isolate nonradiative energy transfer, other than optical absorptive mechanisms, with the effective QD excited state lifetime reducing from 18.0 ns to 13.3 ns with bR integration, demonstrating the Förster resonance energy transfer contributes to 26.1% of the transferred QD energy at the 3.5 nm separation distance. The established direct energy transfer mechanism holds the potential to enhance the bR spectral range and sensitivity of energies that the protein can utilize, increasing its subsequent photocurrent generation, a significant potential expansion of the applicability of bR in solar cell, biosensing, biocomputing, optoelectronic, and imaging technologies.

No MeSH data available.


Related in: MedlinePlus