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

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Mechanistic studies on the flavin: NADH reductase (PrnF) from Pseudomonas fluorescens involved in arylamine oxygenation. / Tiwari, Manish Kumar; Singh, Raushan Kumar; Lee, Jung-Kul; Zhao, Huimin.

I: Bioorganic & Medicinal Chemistry Letters, 2012.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Tiwari, MK, Singh, RK, Lee, J-K & Zhao, H 2012, 'Mechanistic studies on the flavin: NADH reductase (PrnF) from Pseudomonas fluorescens involved in arylamine oxygenation', Bioorganic & Medicinal Chemistry Letters.

APA

Tiwari, M. K., Singh, R. K., Lee, J-K., & Zhao, H. (2012). Mechanistic studies on the flavin: NADH reductase (PrnF) from Pseudomonas fluorescens involved in arylamine oxygenation. Bioorganic & Medicinal Chemistry Letters.

Vancouver

Tiwari MK, Singh RK, Lee J-K, Zhao H. Mechanistic studies on the flavin: NADH reductase (PrnF) from Pseudomonas fluorescens involved in arylamine oxygenation. Bioorganic & Medicinal Chemistry Letters. 2012.

Author

Tiwari, Manish Kumar ; Singh, Raushan Kumar ; Lee, Jung-Kul ; Zhao, Huimin. / Mechanistic studies on the flavin: NADH reductase (PrnF) from Pseudomonas fluorescens involved in arylamine oxygenation. I: Bioorganic & Medicinal Chemistry Letters. 2012.

Bibtex

@article{6adab9fce223431baceaabbc89bf22a7,
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 FADH2 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.",
author = "Tiwari, {Manish Kumar} and Singh, {Raushan Kumar} and Jung-Kul Lee and Huimin Zhao",
year = "2012",
language = "English",
journal = "Bioorganic & Medicinal Chemistry Letters",
issn = "0960-894X",
publisher = "Pergamon Press",

}

RIS

TY - JOUR

T1 - Mechanistic studies on the flavin: NADH reductase (PrnF) from Pseudomonas fluorescens involved in arylamine oxygenation

AU - Tiwari, Manish Kumar

AU - Singh, Raushan Kumar

AU - Lee, Jung-Kul

AU - Zhao, Huimin

PY - 2012

Y1 - 2012

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 FADH2 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 FADH2 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.

M3 - Journal article

JO - Bioorganic & Medicinal Chemistry Letters

JF - Bioorganic & Medicinal Chemistry Letters

SN - 0960-894X

ER -

ID: 229903528