Literature DB >> 9285065

Nonenzymatic reduction of brucine N-oxide by the heme group of cytochrome P450.

K Takekawa1, K Sugihara, S Kitamura, K Tatsumi.   

Abstract

Evidence showing that cytochrome P450-mediated reduction of brucine N-oxide to brucine by rat liver microsomes proceeds nonenzymatically in the presence of both a reduced pyridine nucleotide and FAD is presented. The microsomal N-oxide reduction appears to proceed in two steps: The first step is reduction of FAD by NADPH or NADH either enzymatically or nonenzymatically. The second step is nonenzymatic reduction of the tertiary amine N-oxide by the reduced flavin and is nonenzymatically catalyzed by the heme group of cytochrome P450.

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Year:  1997        PMID: 9285065     DOI: 10.1080/15216549700203421

Source DB:  PubMed          Journal:  Biochem Mol Biol Int        ISSN: 1039-9712


  2 in total

1.  Molecular structure and electron distribution of 4-nitropyridine N-oxide: Experimental and theoretical study of substituent effects.

Authors:  Natalya V Belova; Oleg A Pimenov; Vitaliya E Kotova; Georgiy V Girichev
Journal:  J Mol Struct       Date:  2020-05-17       Impact factor: 3.196

2.  The molecular structure of 4-methylpyridine-N-oxide: Gas-phase electron diffraction and quantum chemical calculations.

Authors:  Natalya V Belova; Georgiy V Girichev; Vitaliya E Kotova; Kseniya A Korolkova; Nguyen Hoang Trang
Journal:  J Mol Struct       Date:  2017-11-17       Impact factor: 3.196

  2 in total

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