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252 related items for PubMed ID: 8663185
1. Is the NAD(P)H:flavin oxidoreductase from Escherichia coli a member of the ferredoxin-NADP+ reductase family?. Evidence for the catalytic role of serine 49 residue. Nivière V, Fieschi F, Décout JL, Fontecave M. J Biol Chem; 1996 Jul 12; 271(28):16656-61. PubMed ID: 8663185 [Abstract] [Full Text] [Related]
2. Cys5 and Cys214 of NAD(P)H:flavin oxidoreductase from Escherichia coli are located in the active site. Fieschi F, Nivière V, Fontecave M. Eur J Biochem; 1996 May 01; 237(3):870-5. PubMed ID: 8647136 [Abstract] [Full Text] [Related]
3. Free flavins accelerate release of ferrous iron from iron storage proteins by both free flavin-dependent and -independent ferric reductases in Escherichia coli. Satoh J, Kimata S, Nakamoto S, Ishii T, Tanaka E, Yumoto S, Takeda K, Yoshimura E, Kanesaki Y, Ishige T, Tanaka K, Abe A, Kawasaki S, Niimura Y. J Gen Appl Microbiol; 2020 Jan 31; 65(6):308-315. PubMed ID: 31281172 [Abstract] [Full Text] [Related]
4. Reaction of the NAD(P)H:flavin oxidoreductase from Escherichia coli with NADPH and riboflavin: identification of intermediates. Nivière V, Vanoni MA, Zanetti G, Fontecave M. Biochemistry; 1998 Aug 25; 37(34):11879-87. PubMed ID: 9718311 [Abstract] [Full Text] [Related]
5. Crystal structure of NAD(P)H:flavin oxidoreductase from Escherichia coli. Ingelman M, Ramaswamy S, Nivière V, Fontecave M, Eklund H. Biochemistry; 1999 Jun 01; 38(22):7040-9. PubMed ID: 10353815 [Abstract] [Full Text] [Related]
6. The NAD(P)H:flavin oxidoreductase from Escherichia coli. Evidence for a new mode of binding for reduced pyridine nucleotides. Nivière V, Fieschi F, Dećout JL, Fontecave M. J Biol Chem; 1999 Jun 25; 274(26):18252-60. PubMed ID: 10373427 [Abstract] [Full Text] [Related]
7. The mechanism and substrate specificity of the NADPH:flavin oxidoreductase from Escherichia coli. Fieschi F, Nivière V, Frier C, Décout JL, Fontecave M. J Biol Chem; 1995 Dec 22; 270(51):30392-400. PubMed ID: 8530465 [Abstract] [Full Text] [Related]
8. 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. Aliverti A, Bruns CM, Pandini VE, Karplus PA, Vanoni MA, Curti B, Zanetti G. Biochemistry; 1995 Jul 04; 34(26):8371-9. PubMed ID: 7677850 [Abstract] [Full Text] [Related]
9. Role of Ser457 of NADPH-cytochrome P450 oxidoreductase in catalysis and control of FAD oxidation-reduction potential. Shen AL, Kasper CB. Biochemistry; 1996 Jul 23; 35(29):9451-9. PubMed ID: 8755724 [Abstract] [Full Text] [Related]
10. Vibrio harveyi NADPH-FMN oxidoreductase arg203 as a critical residue for NADPH recognition and binding. Wang H, Lei B, Tu SC. Biochemistry; 2000 Jul 04; 39(26):7813-9. PubMed ID: 10869187 [Abstract] [Full Text] [Related]
12. The role of a conserved serine residue within hydrogen bonding distance of FAD in redox properties and the modulation of catalysis by Ca2+/calmodulin of constitutive nitric-oxide synthases. Panda SP, Gao YT, Roman LJ, Martásek P, Salerno JC, Masters BS. J Biol Chem; 2006 Nov 10; 281(45):34246-57. PubMed ID: 16966328 [Abstract] [Full Text] [Related]
15. The C-terminal extension of bacterial flavodoxin-reductases: involvement in the hydride transfer mechanism from the coenzyme. Bortolotti A, Sánchez-Azqueta A, Maya CM, Velázquez-Campoy A, Hermoso JA, Medina M, Cortez N. Biochim Biophys Acta; 2014 Jan 10; 1837(1):33-43. PubMed ID: 24016470 [Abstract] [Full Text] [Related]
17. The flavin reductase activity of the flavoprotein component of sulfite reductase from Escherichia coli. A new model for the protein structure. Eschenbrenner M, Covès J, Fontecave M. J Biol Chem; 1995 Sep 01; 270(35):20550-5. PubMed ID: 7657631 [Abstract] [Full Text] [Related]
18. The NAD(P)H:flavin oxidoreductase from Escherichia coli as a source of superoxide radicals. Gaudu P, Touati D, Nivière V, Fontecave M. J Biol Chem; 1994 Mar 18; 269(11):8182-8. PubMed ID: 8132544 [Abstract] [Full Text] [Related]
19. Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module. Gruez A, Pignol D, Zeghouf M, Covès J, Fontecave M, Ferrer JL, Fontecilla-Camps JC. J Mol Biol; 2000 May 26; 299(1):199-212. PubMed ID: 10860732 [Abstract] [Full Text] [Related]