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

doi:10.1002/cbic.200600510

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

Institute of Chemistry

Research output: Contribution to journal › Article › peer-review

49 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 language	English
Pages (from-to)	277-281
Number of pages	5
Journal	ChemBioChem
Volume	8
Issue number	3
DOIs	https://doi.org/10.1002/cbic.200600510
State	Published - 12 Feb 2007

Keywords

Cytochrome P450
Density functional calculations
Enzyme catalysis
Heme proteins
Oxygenation

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10.1002/cbic.200600510

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

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.",

keywords = "Cytochrome P450, Density functional calculations, Enzyme catalysis, Heme proteins, Oxygenation",

author = "Yong Wang and Chuanlu Yang and Hongming Wang and Keli Han and Sason Shaik",

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T2 - Bulk polarity of the active site makes a difference

AU - Wang, Yong

AU - Yang, Chuanlu

AU - Wang, Hongming

AU - Han, Keli

AU - Shaik, Sason

PY - 2007/2/12

Y1 - 2007/2/12

N2 - (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.

AB - (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.

KW - Cytochrome P450

KW - Density functional calculations

KW - Enzyme catalysis

KW - Heme proteins

KW - Oxygenation

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ER -

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

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Keywords

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