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Plasmonic bio-sensing for the Fenna-Matthews-Olson complex.

Guang-Yin Chen1, Neill Lambert2, Yen-An Shih3

  • 1Department of Physics, National Chung Hsing University, Taichung 402, Taiwan.

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|January 4, 2017
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Summary

Metal nanowire surface plasmons can detect changes in the Fenna-Matthews-Olson (FMO) protein complex. Monitoring scattering spectra reveals excitation transfer rates and FMO complex modifications using single photons.

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Area of Science:

  • Plasmonics
  • Biophysics
  • Quantum Biology

Background:

  • The Fenna-Matthews-Olson (FMO) complex is crucial for efficient light-harvesting in photosynthesis.
  • Understanding excitation energy transfer dynamics within the FMO complex is key to comprehending photosynthetic efficiency.
  • Defects or modifications in the FMO complex can impact energy transfer and photosynthetic function.

Purpose of the Study:

  • To theoretically investigate the potential of metal nanowire surface plasmons for bio-sensing applications.
  • To explore the coupling of surface plasmons with specific sites of the FMO complex.
  • To establish a method for monitoring changes in FMO complex structure and energy transfer dynamics.

Main Methods:

  • Theoretical modeling of metal nanowire surface plasmons coupled to the FMO complex.
  • Simulating changes in excitation transfer rates due to suppressed or disconnected sites within the FMO complex.
  • Analyzing variations in scattering spectra and Fano lineshapes of surface plasmons.

Main Results:

  • Changes in FMO complex site connectivity alter excitation transfer rates, detectable via plasmon scattering spectra.
  • Plasmon-site coupling ratios can enhance the sensitivity of these spectral changes.
  • Fano lineshape analysis indicates a unique role for 'site 5' in the FMO complex.
  • The method allows for single-photon detection of local FMO complex modifications.

Conclusions:

  • Metal nanowire surface plasmons offer a viable tool for bio-sensing of the FMO complex.
  • This approach enables the detection of localized defects or modifications in photosynthetic proteins.
  • The method provides insights into both local and global properties of excitation transfer in biological systems.