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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

QD and bR spectra comparison at equal concentrations. QD absorption (green dashed) and emission (green solid) spectra with the bR absorption spectrum (purple solid, magnified by a factor of 3) strongly overlapping the tailored QD emission.
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fig1: QD and bR spectra comparison at equal concentrations. QD absorption (green dashed) and emission (green solid) spectra with the bR absorption spectrum (purple solid, magnified by a factor of 3) strongly overlapping the tailored QD emission.

Mentions: In the present work, we show that bR molecules and colloidal QDs together have the ability to participate in FRET coupling. The retinal molecule of bR has a strong absorption band which makes it a viable FRET acceptor [24–26], and, as shown in Figure 1, an optically tuned QD can be engineered for maximal overlap between its emission and the bR absorption spectra. For this reason, QD activation of bR via FRET has been of considerable interest in recent years [27–30]. However, previous studies could not distinguish FRET coupling between QDs and bR apart from other energy transfer processes. In the present study, we investigate the effects of QD-bR separation distances and excited state lifetime decay of QDs to establish FRET-mediated energy transfer to bR.


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)

QD and bR spectra comparison at equal concentrations. QD absorption (green dashed) and emission (green solid) spectra with the bR absorption spectrum (purple solid, magnified by a factor of 3) strongly overlapping the tailored QD emission.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3376779&req=5

fig1: QD and bR spectra comparison at equal concentrations. QD absorption (green dashed) and emission (green solid) spectra with the bR absorption spectrum (purple solid, magnified by a factor of 3) strongly overlapping the tailored QD emission.
Mentions: In the present work, we show that bR molecules and colloidal QDs together have the ability to participate in FRET coupling. The retinal molecule of bR has a strong absorption band which makes it a viable FRET acceptor [24–26], and, as shown in Figure 1, an optically tuned QD can be engineered for maximal overlap between its emission and the bR absorption spectra. For this reason, QD activation of bR via FRET has been of considerable interest in recent years [27–30]. However, previous studies could not distinguish FRET coupling between QDs and bR apart from other energy transfer processes. In the present study, we investigate the effects of QD-bR separation distances and excited state lifetime decay of QDs to establish FRET-mediated energy transfer to bR.

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