Mechanistic studies on the flavin:NADH reductase (PrnF) from Pseudomonas fluorescens involved in arylamine oxygenation

Manish Kumar Tiwari; Raushan Kumar Singh; Jung Kul Lee; Huimin Zhao

doi:10.1016/j.bmcl.2011.12.078

Mechanistic studies on the flavin:NADH reductase (PrnF) from Pseudomonas fluorescens involved in arylamine oxygenation

Manish Kumar Tiwari, Raushan Kumar Singh, Jung Kul Lee, Huimin Zhao

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Abstract

We report the mechanistic studies of a FAD:NADH reductase (PrnF) involved in arylamine oxygenation. PrnF catalyzes the reduction of FAD via a sequential ordered bi-bi mechanism with NADH as the first substrate to bind and FADH ₂ as the first product to be released. The residues Asp145 and His146 are proposed as catalytic acid/base residues for PrnF based on pH profile and molecular dynamics simulation studies. These studies provide the first detailed account of the mechanism of the flavin reductase involved in arylamine oxygenation.

Original language	English (US)
Pages (from-to)	1344-1347
Number of pages	4
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	22
Issue number	3
DOIs	https://doi.org/10.1016/j.bmcl.2011.12.078
State	Published - Feb 1 2012

Keywords

Arylamine oxygenation
FAD:NADH reductase
Reaction mechanism

ASJC Scopus subject areas

Pharmaceutical Science
Drug Discovery
Organic Chemistry
Molecular Medicine
Molecular Biology
Clinical Biochemistry
Biochemistry

Online availability

10.1016/j.bmcl.2011.12.078

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title = "Mechanistic studies on the flavin:NADH reductase (PrnF) from Pseudomonas fluorescens involved in arylamine oxygenation",

abstract = "We report the mechanistic studies of a FAD:NADH reductase (PrnF) involved in arylamine oxygenation. PrnF catalyzes the reduction of FAD via a sequential ordered bi-bi mechanism with NADH as the first substrate to bind and FADH 2 as the first product to be released. The residues Asp145 and His146 are proposed as catalytic acid/base residues for PrnF based on pH profile and molecular dynamics simulation studies. These studies provide the first detailed account of the mechanism of the flavin reductase involved in arylamine oxygenation.",

keywords = "Arylamine oxygenation, FAD:NADH reductase, Reaction mechanism",

author = "Tiwari, {Manish Kumar} and Singh, {Raushan Kumar} and Lee, {Jung Kul} and Huimin Zhao",

note = "Funding Information: This work was supported by the 21C Frontier Microbial Genomics and Applications Center Program (J.-K.L.), and the National Research Foundation grant (NRF 220-2009-1-D00033) (J.-K.L.) funded by the Korea government (MEST), and a grant from the Office of Naval Research (N00014-02-1-0725) (H.Z.). ",

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AU - Tiwari, Manish Kumar

AU - Singh, Raushan Kumar

AU - Lee, Jung Kul

AU - Zhao, Huimin

N1 - Funding Information: This work was supported by the 21C Frontier Microbial Genomics and Applications Center Program (J.-K.L.), and the National Research Foundation grant (NRF 220-2009-1-D00033) (J.-K.L.) funded by the Korea government (MEST), and a grant from the Office of Naval Research (N00014-02-1-0725) (H.Z.).

PY - 2012/2/1

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N2 - We report the mechanistic studies of a FAD:NADH reductase (PrnF) involved in arylamine oxygenation. PrnF catalyzes the reduction of FAD via a sequential ordered bi-bi mechanism with NADH as the first substrate to bind and FADH 2 as the first product to be released. The residues Asp145 and His146 are proposed as catalytic acid/base residues for PrnF based on pH profile and molecular dynamics simulation studies. These studies provide the first detailed account of the mechanism of the flavin reductase involved in arylamine oxygenation.

AB - We report the mechanistic studies of a FAD:NADH reductase (PrnF) involved in arylamine oxygenation. PrnF catalyzes the reduction of FAD via a sequential ordered bi-bi mechanism with NADH as the first substrate to bind and FADH 2 as the first product to be released. The residues Asp145 and His146 are proposed as catalytic acid/base residues for PrnF based on pH profile and molecular dynamics simulation studies. These studies provide the first detailed account of the mechanism of the flavin reductase involved in arylamine oxygenation.

KW - Arylamine oxygenation

KW - FAD:NADH reductase

KW - Reaction mechanism

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JO - Bioorganic and Medicinal Chemistry Letters

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Mechanistic studies on the flavin:NADH reductase (PrnF) from Pseudomonas fluorescens involved in arylamine oxygenation

Abstract

Keywords

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