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Electron transfer in ruthenium-modified proteins

M J Bjerrum1, D R Casimiro, I J Chang

  • 1California Institute of Technology, Pasadena 91125, USA.

Journal of Bioenergetics and Biomembranes
|June 1, 1995
PubMed
Summary

Photochemical methods reveal electron transfer (ET) kinetics in modified proteins. Electron transfer rates in Ru-modified cytochromes and azurins show distance dependence, aligning with tunneling-pathway models.

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Area of Science:

  • Biophysical Chemistry
  • Photochemistry
  • Protein Electron Transfer

Background:

  • Intramolecular electron transfer (ET) is crucial in biological systems.
  • Ruthenium complexes (Ru) are widely used as labels for studying ET in proteins.
  • Cytochrome c and azurin are important metalloproteins for electron transfer studies.

Purpose of the Study:

  • To measure the kinetics of intramolecular electron transfer in Ru-modified cytochrome c and azurin.
  • To investigate the driving-force effects on Fe2+-->Ru3+ ET reactions.
  • To analyze the distance dependence of ET in various Ru-modified proteins.

Main Methods:

  • Photochemical techniques were employed to initiate and measure electron transfer.
  • Driving-force studies were conducted using His33 derivatives of cytochrome c.

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  • A tunneling-pathway model was used to analyze distance-dependent ET rates.

    • Main Results:

    • Reorganization energy (lambda) for Fe2+-->Ru3+ ET in His33 cytochrome c was determined to be 0.8 eV.
    • Anomalously fast reductions of ferriheme suggest potential electronically excited ferroheme formation.
    • ET rates in 10 out of 12 Ru-modified systems showed exponential dependence on metal-metal separation (decay constant 1.06 A-1).

    Conclusions:

    • The observed distance dependence of ET rates is consistent with the predictions of the tunneling-pathway model.
    • Ruthenium modification provides a valuable tool for dissecting electron transfer mechanisms in metalloproteins.
    • Further studies are warranted to explore the role of excited states in rapid electron transfer events.