Interfacial Electron Transfer Reactions of Heme Proteins

  • Yuan Xiaoling
  • John K. Cullison
  • Songcheng Sun
  • Fred M. Hawkridge


The kinetics and thermodynamics of electron transfer reactions of heme proteins can be studied directly at metal and semiconductor electrodes. We have been interested in characterizing the heterogeneous electron transfer properties of biological electron transfer proteins since the initial report of electrocatalysis in the reaction of spinach ferredoxin at a polymer modified gold electrode (Landrum et al., 1977). This 11,000 dalton iron-sulfur protein, which participates in green plant photosynthesis, was shown to undergo direct, heterogeneous, electron transfer at quasi- reverisble rates at this modified electrode. Later that year two communications described quasi-reversible electron transfer rates by cytochrome c at modified gold (Eddowes and Hill, 1977) and at bare indium oxide (Yeh and Kuwana, 1977) electrodes.


Formal Potential Electron Transfer Reaction Break Temperature Indium Oxide Heme Protein 
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Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • Yuan Xiaoling
    • 1
  • John K. Cullison
    • 1
  • Songcheng Sun
    • 1
  • Fred M. Hawkridge
    • 1
  1. 1.Department of ChemistryVirginia Commonwealth UniversityRichmondUSA

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