NAD(P)H‐flavin oxidoreductase from the bioluminescent bacterium, Vibrio fischeri ATCC 7744, is a flavoprotein

FEBS Letters

Inouye, Satoshi¹ 

[1] Yokohama Research Center, Chisso Corp., Kanazawa-ku, Yokohama 236, Japan

关键词: Reduced flavin;    Bacterial luciferase;    NADH oxidase;    Nitroreductase;    Diaphorase;   

DOI  :  10.1016/0014-5793(94)00528-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The NAD(P)H-flavin oxidoreductase gene from the bioluminescent bacterium, Vibrio fischeri ATCC 7744, was expressed in Escherichia coli, and the enzyme purified using Cibacron Blue 3G-A affinity column chromatography from crude extracts in a single step. The purified enzyme had a typical flavoprotein absorption spectrum and flavin mononucleotide (FMN) was identified as a prosthetic group, non-covalently bound in a molar ratio of 1:1. The enzyme catalyzed the electron transfer from NADH via FMNH₂ to various other electron acceptors. Reduced flavin produced by flavin reductase participated non-enzymatically in the following reactions: H₂O₂-forming NADH oxidase-like, oxygen-insenstive nitroreductase-like, diaphorase (quinone reductase)-like and bacterial luciferase reactions.

【 授权许可】

Unknown