A new mechanism for ethanol oxidation mediated by cytochrome P450 2E1: Bulk polarity of the active site makes a difference

Yong Wang, Chuanlu Yang, Hongming Wang, Keli Han*, Sason Shaik

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

48 Scopus citations

Abstract

(Figure Presented) Breaking the habit. A new mechanism, called reversed dual hydrogen abstraction (R-DHA), is presented for ethanol oxidation by cytochrome P450 2E1 (CYP2E1). It is shown that the competition of R-DHA with the consensus mechanism (gem-diol) is modulated by the ethanol population in the enzyme pocket. Thus, as a response to growing blood ethanol level, CYP2E1 adapts its ethanol metabolism by a mechanistic switch from gem-diol to R-DHA.

Original languageEnglish
Pages (from-to)277-281
Number of pages5
JournalChemBioChem
Volume8
Issue number3
DOIs
StatePublished - 12 Feb 2007

Keywords

  • Cytochrome P450
  • Density functional calculations
  • Enzyme catalysis
  • Heme proteins
  • Oxygenation

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