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Electrochemistry of Cytochrome P450 BM3 in Sodium Dodecyl Sulfate Films
Langmuir (2006)
  • Andrew K Udit
  • Michael G Hill
  • Harry B Gray
Direct electrochemistry of the cytochrome P450 BM3 heme domain (BM3) was achieved by confining the protein within sodium dodecyl sulfate (SDS) films on the surface of basal-plane graphite (BPG) electrodes. Cyclic voltammetry revealed the heme FeIII/II redox couple at −330 mV (vs Ag/AgCl, pH 7.4). Up to 10 V/s, the peak current was linear with the scan rate, allowing us to treat the system as surface-confined within this regime. The standard heterogeneous rate constant determined at 10 V/s was estimated to be 10 s-1. Voltammograms obtained for the BM3−SDS−BPG system in the presence of dioxygen exhibited catalytic waves at the onset of FeIII reduction. The altered heme reduction potential of the BM3−SDS−graphite system indicates that SDS is likely bound in the enzyme active-site region. Compared to other P450-surfactant systems, we find redox potentials and electron-transfer rates that differ by ∼ 100 mV and >10-fold, respectively, indicating that the nature of the surfactant environment has a significant effect on the observed heme redox properties.
Publication Date
September 2, 2006
Citation Information
Andrew K Udit, Michael G Hill and Harry B Gray. "Electrochemistry of Cytochrome P450 BM3 in Sodium Dodecyl Sulfate Films" Langmuir Vol. 22 Iss. 25 (2006)
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