Mechanistic studies on the flavin:NADH reductase (PrnF) from Pseudomonas fluorescens involved in arylamine oxygenation.
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.
Department of Chemical Engineering, Konkuk University, Seoul 143-701, Republic of Korea.
Manish Kumar
MK
Tiwari
Raushan Kumar
RK
Singh
Jung-Kul
JK
Lee
Huimin
H
Zhao
D000588:Amines / Q000378:metabolism; D001665:Binding Sites; D038181:FMN Reductase / Q000737:chemistry* / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D006899:Mixed Function Oxygenases / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D015394:Molecular Structure; D010100:Oxygen / Q000737:chemistry; D011551:Pseudomonas fluorescens / Q000201:enzymology*
D000588:Amines; D006899:Mixed Function Oxygenases; C035198:arylamine N-hydroxylase; D038181:FMN Reductase; D010100:Oxygen