NAD(P)H-flavin oxidoreductase from the bioluminescent bacterium, Vibrio fischeri ATCC 7744, is a flavoprotein.
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-insensitive nitroreductase-like, diaphorase (quinone reductase)-like and bacterial luciferase reactions.
Inouye
S
S
Yokohama Research Center, Chisso Corp., Japan.
D000595:Amino Acid Sequence; D002846:Chromatography, Affinity; D004579:Electron Transport; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D004926:Escherichia coli; D038181:FMN Reductase; D005486:Flavin Mononucleotide / Q000032:analysis / Q000737:chemistry / Q000378:metabolism; D006358:Hot Temperature; D006861:Hydrogen Peroxide / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D049449:Luminescence; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009243:NAD / Q000378:metabolism; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins; D013053:Spectrophotometry; D014733:Vibrio / Q000201:enzymology*
D011994:Recombinant Proteins; D009243:NAD; D005486:Flavin Mononucleotide; D006861:Hydrogen Peroxide; D038181:FMN Reductase; D009247:NADH, NADPH Oxidoreductases