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Intermolecular biological electron transfer: an electrochemical approach.

Katsumi Niki1, James R Sprinkle, Emanuel Margoliash

  • 1Beckman Institute, California Institute of Technology, Pasadena, CA 91125, USA. kniki@bilrc.caltech.edu

Bioelectrochemistry (Amsterdam, Netherlands)
|January 12, 2002
PubMed
Summary
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Electron transfer rates between gold electrodes and immobilized cytochrome c depend on alkanethiol chain length. Short chains limit electron transfer due to a protein rearrangement, suggesting lysine-13 is crucial for efficient electron transfer.

Area of Science:

  • Electrochemistry
  • Biophysics
  • Surface Science

Background:

  • Cytochrome c is a key protein in cellular respiration and electron transfer.
  • Self-assembled monolayers (SAMs) are widely used to functionalize electrode surfaces.
  • Understanding electron transfer at bio-electrode interfaces is crucial for biosensor development.

Purpose of the Study:

  • To investigate electron transfer (ET) rates between a gold electrode and immobilized cytochrome c.
  • To determine the influence of alkanethiol chain length on ET rates.
  • To elucidate the mechanism of rate limitation in short-chain alkanethiols.

Main Methods:

  • Potential modulated electroreflectance spectroscopy was used to measure ET rates.
  • Cytochrome c was immobilized on gold electrodes via alkanethiol SAMs with varying chain lengths.

Related Experiment Videos

  • A mutant cytochrome c (RC9-K13A) was used to probe the role of lysine-13.
  • Main Results:

    • Electron transfer rates showed a linear dependence on chain length for long alkanethiols.
    • Electron transfer rates became independent of chain length for short alkanethiols.
    • A mutant cytochrome c with lysine-13 replaced by alanine exhibited ET rates over six orders of magnitude lower than native cytochrome c.

    Conclusions:

    • Electron transfer through short alkyl chains is limited by a protein conformational rearrangement preceding the ET event.
    • This rearrangement, termed "gating," involves cytochrome c shifting to a configuration that facilitates efficient ET pathways.
    • Lysine-13 of cytochrome c is proposed to be critical for facilitating efficient electron transfer to the carboxylate terminus.