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Related Experiment Videos

Long-range electron transfer in myoglobin.

J A Cowan1, R K Upmacis, D N Beratan

  • 1Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.

Annals of the New York Academy of Sciences
|January 1, 1988
PubMed
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This study quantifies electron transfer (ET) in modified myoglobins, revealing key electronic coupling parameters and reorganization energy. Findings illuminate protein-mediated electron tunneling pathways.

Area of Science:

  • Biophysical Chemistry
  • Protein Electron Transfer
  • Bioinorganic Chemistry

Background:

  • Myoglobin's heme group is crucial for its biological function.
  • Understanding electron transfer (ET) in proteins is vital for bioenergetics and biomimetic design.
  • Surface-ruthenated myoglobins offer a model system to study protein-mediated ET.

Purpose of the Study:

  • To investigate the distance and driving-force dependences of electron transfer (ET) in surface-ruthenated myoglobins.
  • To determine the magnitude and decay of protein-mediated electronic coupling.
  • To estimate reorganization energy and evaluate specific electron-tunneling pathways.

Main Methods:

  • Systematic replacement of the heme prosthetic group with metalloporphyrins of varying redox potentials.

Related Experiment Videos

  • Analysis of electron transfer rates as a function of distance and driving force.
  • Application of a rate expression incorporating electron-vibration coupling to classical and quantum mechanical modes.

    • Main Results:

    • Quantified the magnitude of electronic coupling (Hab ≈ 6.3 x 10^-3 cm^-1 at 12.7 Å) and its decay (β ≈ 0.8 Å^-1).
    • Estimated a reorganization energy (λ ≈ 1.3 eV), with ~0.7 eV attributed to the porphyrin and peptide matrix.
    • Evaluated specific electron-tunneling pathways within the protein structure.

    Conclusions:

    • Established quantitative parameters for protein-mediated electronic coupling in myoglobin.
    • Provided insights into the energetic contributions to reorganization during electron transfer.
    • Demonstrated the utility of modified myoglobins for elucidating electron tunneling mechanisms in proteins.