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References
Gerlo, E.; Charlier, J.: Identification of NADH-specific and NADPH-specific FMN reductases in Beneckea harveyi. Eur. J. Biochem., 57, 461–467 (1975)
Jablonski, E.; DeLuca, M.: Purification and properties of the NADH and NADPH specific FMN oxidoreductases from Beneckea harveyi. Biochemistry, 16, 2932–2936 (1977)
Michaliszyn, G.A.; Wing, S.S.; Meighen, E.A.: Purification and properties of a NAD(P)H:flavin oxidoreductase from the luminous bacterium, Benecka harveyi. J. Biol. Chem., 252, 7495–7499 (1977)
Spencer, R.; Fisher, J.; Walsh, C.: Reconstitution of flavin enzymes with 1-carba-1-deazaflavin coenzyme analogues. Biochemistry, 16, 3594–3602 (1977)
Yubisui, T.; Matsuki, T.; Tanishima, K.; Takeshita, M.; Yoneyama, Y.: NADPH-flavin reductase in human erythrocytes and the reduction of methemoglobin through flavin by the enzyme. Biochem. Biophys. Res. Commun., 76, 174–183 (1977)
Hasan, N.; Nester, E.W.: Purification and characterization of NADPH-dependent flavin reductase. J. Biol. Chem., 253, 4987–4992 (1978)
Jablonski, E.; DeLuca, M.: Studies of the control of luminescence in Beneckea harveyi: Properties of the NADH and NADPHtFMN oxidoreductases. Biochemistry, 17, 672–679 (1978)
Walsh, C.; Fisher, J.; Spencer, R.; Graham, D.W.; Ashton, W.T.; Brown, J.E.; Brown, R.D.; Rogers, E.F.: Chemical and enzymatic properties of riboflavin analogues. Biochemistry, 17, 1942–1951 (1978)
Feighner, S.D.; Bokkenheuser, V.D.; Winter, J.; Hylemon, P.B.: Characterization of a C21 neutral steroid hormone transforming enzyme, 21-dehydroxylase, in crude cell extracts of Eubacterium lentum. Biochim. Biophys. Acta, 574, 154–163 (1979)
Yubisui, T.; Matsuki, T.; Takeshita, M.; Yoneyama, Y.: Characterization of the purified NADPH-flavin reductase of human erythrocytes. J. Biochem., 85, 719–728 (1979)
Nefsky, B.; DeLuca, M.: Studies on the NADH and NADPH: riboflavin 5′-phosphate (FMN) oxidoreductases from Beneckea harveyi: Characterization of the FMN binding sites. Arch. Biochem. Biophys., 216, 10–16 (1982)
Fontecave, M.; Eliasson, R.; Reichard, P.: NAD(P)H:flavin oxidoreductase of Escherichia coli. J. Biol. Chem., 262, 12325–12331 (1987)
Quandt, K.S.; Xu, F.; Chen, P.; Hultquist, D.E.: Evidence that the protein components of bovine erythrocyte green heme binding protein and flavin reductase are identical. Biochem. Biophys. Res. Commun., 178, 315–321 (1991)
Spyrou, G.; Haggard-Ljungquist, E.; Krook, M.; Joernvall, H.; Nilsson, E.; Reichard, P.: Characterization of the flavin reductase gene (fre) of Escherichia coli and construction of a plasmid for overproduction of the enzyme. J. Bacteriol., 173, 3673–3679 (1991)
Coves, J.; Niviere, V.; Eschenbrenner, M.; Fontecave, M.: NADPH-Sulfite reductase from Escherichia coli. A flavin reductase participating in the generation of the free radical of ribonucleotide reductase. J. Biol. Chem., 268, 18604–18609 (1993)
Inouye, S.: NAD(P)H:flavin oxidoreductase from the bioluminescent bacterium, Vibrio fischeri ATCC 7744, is a flavoprotein. FEBS Lett., 347, 163–168 (1994)
Inouye, S.; Nakamura, H.: Stereospecificity of hydride transfer and substrate specificity for FMN-containing NAD(P)H:flavin oxidoreductase from the luminescent bacterium, Vibrio fischeri ATCC 7744. Biochem. Biophys. Res. Commun., 205, 275–281 (1994)
Fieschi, F.; Niviere, V.; Frier, C.; Decout, J.L.; Fontecave, M.: The mechanism and substrate specificity of the NADPH:flavin oxidoreductase from Escherichia coli. J. Biol. Chem., 270, 30392–30400 (1995)
Niviere, V.; Fieschi, F.; Decout, J.L.; Fontecave, M.: Is the NAD(P)H:flavin oxidoreductase from Escherichia coli a member of the ferredoxin-NADP+ reductase family?. J. Biol. Chem., 271, 16656–16661 (1996)
Bruchhaus, I.; Richter, S.; Tannich, E.: Recombinant expression and biochemical characterization of an NADPH:flavin oxidoreductase from Entamoeba histolytica. Biochem. J., 330, 1217–1221 (1998)
Koike, H.; Sasaki, H.; Kobori, T.; Zenno, S.; Saigo, K.; Murphy, M.E.P.; Adman, E.T.; Tanokura, M.: 1.8 A crystal structure of the major NAD(P)H:FMN oxidoreductase of a bioluminescent bacterium, Vibrio fischeri: Overall structure, cofactor and substrate-analog binding, and comparison with related flavoproteins. J. Mol. Biol., 280, 259–273 (1998)
Lei, B.; Tu, S.C.: Mechanism of reduced flavin transfer from Vibrio harveyi NADPH-FMN oxidoreductase to luciferase. Biochemistry, 37, 14623–14629 (1998)
Niviere, V.; Vanoni, M.A.; Zanetti, G.; Fontecave, M.: Reaction of the NAD(P)H:flavin oxidoreductase from Escherichia coli with NADPH and riboflavin: Identification of intermediates. Biochemistry, 37, 11879–11887 (1998)
Ingelman, M.; Ramaswamy, S.; Niviere, V.; Fontecave, M.; Eklund, H.: Crystal structure of NAD(P)H:flavin oxidoreductase from Escherichia coli. Biochemistry, 38, 7040–7049 (1999)
Min, D.J.; Andrade, J.D.; Stewart, R.J.: Specific immobilization of in vivo biotinylated bacterial luciferase and FMN:NAD(P)H oxidoreductase. Anal. Biochem., 270, 133–139 (1999)
Niviere, V.; Fieschi, F.; Decout, J.L.; Fontecave, M.: The NAD(P)H:flavin oxidoreductase from Escherichia coli. Evidence for a new mode of binding for reduced pyridine nucleotides. J. Biol. Chem., 274, 18252–18260 (1999)
Tang, C.K.; Jeffers, C.E.; Nichols, J.C.; Tu, S.C.: Flavin specificity and subunit interaction of Vibrio fischeri general NAD(P)H-flavin oxidoreductase FRG/FRase I. Arch. Biochem. Biophys., 392, 110–116 (2001)
Riefler, R.G.; Smets, B.F.: NAD(P)H:flavin mononucleotide oxidoreductase inactivation during 2,4,6-trinitrotoluene reduction. Appl. Environ. Microbiol., 68, 1690–1696 (2002)
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(2005). FMN Redctase. In: Schomburg, D., Schomburg, I. (eds) Springer Handbook of Enzymes. Springer Handbook of Enzymes, vol 23. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-37648-8_29
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DOI: https://doi.org/10.1007/3-540-37648-8_29
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