J. Covès and M. Fontecave, Reduction and mobilization of iron by a NAD(P)H: flavin oxidoreductase from Escherichia coli, European Journal of Biochemistry, vol.26, issue.3, pp.635-641, 1993.
DOI : 10.1016/0166-6851(80)90045-6

M. Fontecave, P. Nordlund, H. Eklund, R. , and P. , Adv, 1992.

B. Lei, M. Liu, S. Huang, T. , and S. C. , Vibrio harveyi NADPH-flavin oxidoreductase: cloning, sequencing and overexpression of the gene and purification and characterization of the cloned enzyme., Journal of Bacteriology, vol.176, issue.12, pp.3552-3558, 1994.
DOI : 10.1128/jb.176.12.3552-3558.1994

S. Zenno, K. Saigo, H. Kanoh, and S. Inouye, Identification of the gene encoding the major NAD(P)H-flavin oxidoreductase of the bioluminescent bacterium Vibrio fischeri ATCC 7744., Journal of Bacteriology, vol.176, issue.12, pp.3536-3543, 1994.
DOI : 10.1128/jb.176.12.3536-3543.1994

K. A. Gray, O. S. Pogrebinsky, G. T. Mrachko, L. Xi, D. J. Monticello et al., Molecular mechanisms of biocatalytic desulfurization of fossil fuels, Nature Biotechnology, vol.14, issue.13, pp.1705-1709, 1996.
DOI : 10.1146/annurev.mi.46.100192.001205

V. Blanc, D. Lagneaux, P. Didier, P. Gil, P. Lacroix et al., Cloning and analysis of structural genes from Streptomyces pristinaespiralis encoding enzymes involved in the conversion of pristinamycin IIB to pristinamycin IIA (PIIA): PIIA synthase and NADH:riboflavin 5'-phosphate oxidoreductase., Journal of Bacteriology, vol.177, issue.18, pp.5206-5214, 1995.
DOI : 10.1128/jb.177.18.5206-5214.1995

R. J. Parry, L. , and W. , An NADPH:FAD Oxidoreductase from the Valanimycin Producer,Streptomyces viridifaciens: CLONING, ANALYSIS, AND OVEREXPRESSION, Journal of Biological Chemistry, vol.272, issue.37, pp.23303-23311, 1997.
DOI : 10.1074/jbc.272.37.23303

H. Koike, H. Sasaki, T. Koribo, S. Zenno, K. Saigo et al., 1.8 ?? 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, Journal of Molecular Biology, vol.280, issue.2, pp.259-273, 1998.
DOI : 10.1006/jmbi.1998.1871

URL : https://hal.archives-ouvertes.fr/in2p3-00421359

M. Eschenbrenner, J. Covès, and M. Fontecave, The Flavin Reductase Activity of the Flavoprotein Component of Sulfite Reductase from Escherichia coli: A NEW MODEL FOR THE PROTEIN STRUCTURE, Journal of Biological Chemistry, vol.270, issue.35, pp.20550-20555, 1995.
DOI : 10.1074/jbc.270.35.20550

G. Spyrou, E. Haggard-ljungquist, M. Krook, H. Jornvall, E. Nilsson et al., Characterization of the flavin reductase gene (fre) of Escherichia coli and construction of a plasmid for overproduction of the enzyme., Journal of Bacteriology, vol.173, issue.12, pp.3673-3679, 1991.
DOI : 10.1128/jb.173.12.3673-3679.1991

C. M. Bruns and P. A. Karplus, Refined Crystal Structure of Spinach Ferredoxin Reductase at 1.7 ?? Resolution: Oxidized, Reduced and 2???-Phospho-5???-AMP Bound States, Journal of Molecular Biology, vol.247, issue.1, pp.125-145, 1995.
DOI : 10.1006/jmbi.1994.0127

A. Aliverti, C. M. Bruns, V. E. Pandini, P. A. Karplus, M. A. Vanoni et al., Involvement of Serine 96 in the Catalytic Mechanism of Ferredoxin-NADP+ Reductase: Structure-Function Relationship As Studied by Site-Directed Mutagenesis and X-ray Crystallography, Biochemistry, vol.34, issue.26, pp.8371-8379, 1995.
DOI : 10.1021/bi00026a019

G. Gassner, L. Wang, C. Batie, and D. P. Ballou, Reaction of Phthalate Dioxygenase Reductase with NADH and NAD: Kinetic and Spectral Characterization of Intermediates, Biochemistry, vol.33, issue.40, pp.12184-12193, 1994.
DOI : 10.1021/bi00206a022

G. T. Gassner and D. P. Ballou, Preparation and Characterization of a Truncated Form of Phthalate Dioxygenase Reductase That Lacks an Iron-Sulfur Domain, Biochemistry, vol.34, issue.41, pp.13460-13471, 1995.
DOI : 10.1021/bi00041a025

M. M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Analytical Biochemistry, vol.72, issue.1-2, pp.248-254, 1976.
DOI : 10.1016/0003-2697(76)90527-3

S. B. Mostad and A. Glasfeld, Using high field NMR to determine dehydrogenase stereospecificity with respect to NADH: An undergraduate biochemistry lab, Journal of Chemical Education, vol.70, issue.6, pp.504-506, 1993.
DOI : 10.1021/ed070p504

S. Inouye and H. Nakamura, Stereospecificity of Hydride Transfer and Substrate Specificity for FMN-Containing NAD(P)H-Flavin Oxidoreductase from the Luminescent Bacterium, Vibrio fischeri ATCC 7744, Biochemical and Biophysical Research Communications, vol.205, issue.1, pp.275-281, 1994.
DOI : 10.1006/bbrc.1994.2661

K. Dalziel, . Ed, P. D. Boyer, E. Rudolph, F. B. Fromm et al., The Enzymes, pp.2-59, 1973.

H. J. Fromm, [18] Use of competitive inhibitors to study substrate binding order, Methods Enzymol, vol.63, pp.467-486, 1979.
DOI : 10.1016/0076-6879(79)63020-3

D. S. Sem and C. B. Kasper, Geometric relationship between the nicotinamide and isoalloxazine rings in NADPH-cytochrome P-450 oxidoreductase: implications for the classification of evolutionarily and functionally related flavoproteins, Biochemistry, vol.31, issue.13, pp.3391-3398, 1992.
DOI : 10.1021/bi00128a013

A. Trimboli, J. Barber, M. , and J. , Assimilatory Nitrate Reductase: Reduction and Inhibition by NADH/NAD+ Analogs, Archives of Biochemistry and Biophysics, vol.315, issue.1, pp.48-53, 1994.
DOI : 10.1006/abbi.1994.1469

C. C. Correll, C. J. Batie, D. P. Ballou, and M. L. Ludwig, Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S], Science, vol.258, issue.5088, pp.1604-1610, 1992.
DOI : 10.1126/science.1280857