Electrochemistry of cytochrome P450 BM3 in sodium dodecyl sulfate films.

  • Udit A
  • Hill M
  • Gray H
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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 approximately 100 mV and >10-fold, respectively, indicating that the nature of the surfactant environment has a significant effect on the observed heme redox properties.

Author-supplied keywords

  • Binding Sites
  • Biosensing Techniques
  • Cytochrome P-450 Enzyme System
  • Cytochrome P-450 Enzyme System: chemistry
  • Electrochemistry
  • Electrolysis
  • Graphite
  • Graphite: chemistry
  • Heme
  • Heme: chemistry
  • Membranes, Artificial
  • Oxidation-Reduction
  • Sodium Dodecyl Sulfate
  • Sodium Dodecyl Sulfate: chemistry
  • Structure-Activity Relationship
  • Surface Properties

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  • Andrew K Udit

  • Michael G Hill

  • Harry B Gray

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