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Related Experiment Videos

Redox processes of cytochrome c immobilized on solid supported polyelectrolyte multilayers.

Inez M Weidinger1, Daniel H Murgida, Wen-Fei Dong

  • 1Institut für Chemie, Technische Universität Berlin, Sekr. PC14, Strasse des 17, Juni, D-10623 Berlin, Germany.

The Journal of Physical Chemistry. B
|February 14, 2006
PubMed
Summary

This study used surface-enhanced resonance Raman spectroscopy to investigate immobilized cytochrome c (Cyt-c) on polyelectrolyte multilayers. Findings reveal how Cyt-c

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Area of Science:

  • Electrochemistry
  • Spectroscopy
  • Biophysics

Background:

  • Cytochrome c (Cyt-c) is a crucial heme protein involved in electron transfer.
  • Polyelectrolyte multilayers (PEMs) offer versatile platforms for biomolecule immobilization.
  • Understanding interfacial processes is key for biosensor development.

Purpose of the Study:

  • To probe the redox site structure of immobilized Cyt-c.
  • To elucidate the mechanism and dynamics of potential-dependent interfacial processes.
  • To investigate the influence of PEM composition on Cyt-c behavior.

Main Methods:

  • Stationary and time-resolved surface-enhanced resonance Raman (SERR) spectroscopy.
  • Fabrication of PEMs using polycations (PEI, PAH) and polyanions (PSS).

Related Experiment Videos

  • Electrochemical measurements on Cyt-c immobilized on silver electrodes.

    • Main Results:

    • Cyt-c immobilized on PEI/PSS layers shows peripheral binding and full redox activity with a lowered redox potential.
    • Heterogeneous electron transfer (ET) rate is consistent with tunneling through ordered PEI/PSS layers and coupled to conformational changes.
    • Additional PAH/PSS layers lead to PSS/Cyt-c complex formation, altering redox potential and enhancing ET rates.

    Conclusions:

    • Cyt-c binding to PSS can disrupt PEM structure, with Cyt-c penetrating PAH/PSS layers.
    • Specific PSS/Cyt-c complexes act as efficient gates for heterogeneous electron transfer.
    • PEM architecture significantly influences the electrochemical and conformational properties of immobilized Cyt-c.