Recent progress in cytochrome P450 enzyme electrochemistry

Barry D. Fleming, Daniel L. Johnson, Alan M. Bond, Lisandra L. Martin*

*Corresponding author for this work

Research output: Contribution to journalReview article

36 Citations (Scopus)

Abstract

Cytochrome P450 (CYP) enzymes perform crucial functions in humans, including the metabolism of drugs and hormone synthesis. The catalytic reactions performed by these enzymes (typically monoxygenation) require the transfer of electrons. Thermodynamic and mechanistic detail of the electron transfer component of these catalytic processes has been obtained traditionally from potentiometric titrations. More recently, voltammetric approaches (that are inherently simpler and require less sample) have been used. This has been made possible by the creation of biocompatible electrode surfaces at which the P450 enzyme is confined and able to undergo physiologically relevant electron transfer processes. The continuing challenge has been to obtain an in vivo-like enzyme response, and to provide the basis for the creation of an artificial bioprocess in vitro. A powerful instrumental electrochemical method, employing Fourier-transformed large-amplitude ac voltammetry, offers the potential for greater insight and new opportunities to understand the nuances of the electron transfer process. This review highlights several recent advances in the electrochemistry of P450 enzymes rather than providing a comprehensive review of P450 electrochemistry.

Original languageEnglish
Pages (from-to)581-589
Number of pages9
JournalExpert Opinion on Drug Metabolism and Toxicology
Volume2
Issue number4
DOIs
Publication statusPublished - 2006
Externally publishedYes

Keywords

  • Cytochrome P450
  • Electrochemistry
  • Enzyme
  • Immobilisation
  • Redox potential
  • Voltammetry

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