Structural studies of ferredoxin:NADP⁺ reductase family

Last modified: Wed Apr 14 12:24:12 BST 2004

• Aliverti, A., Lubberstedt, T., Zanetti, G., Herrmann, R.G. and Curti, B. (1991) Probing the role of lysine 116 and lysine 244 in the spinach ferredoxin-NADP⁺ reductase by site-directed mutagenesis. J. Biol. Chem. 266, 17760-17763.
• Aliverti, A., Bruns, C.M., Pandini, V.E., Karplus, P.A., Vanoni, M.A., Curti, B. and Zanetti, G. (1995) 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 34, 8371-8379.
• Aliverti, A., Deng, Z., Ravasi, D., Piubelli, L., Karplus, P.A. and Zanetti, G. (1998) Probing the function of the invariant glutamyl residue 312 in spinach ferredoxin-NADP⁺ reductase. J. Biol. Chem. 273, 34008-34015.
• Bruns, C.M. and Karplus, P.A. (1995) Refined crystal structure of spinach ferredoxin reductase at 1.7 Å resolution: oxidized, reduced and 2´-phospho-5´-AMP bound states. J. Mol. Biol. 247, 125-145.
• Correll, C.C., Batie, C.J., Ballou, D.P. and Ludwig, M.L. (1985) Crystallographic characterization of phthalate oxygenase reductase, an iron-sulfur flavoprotein from Pseudomonas cepacia. J. Biol. Chem. 260, 14633-14635.
• Correll, C.C., Batie, C.J., Ballou, D.P. and Ludwig, M.L. (1992) Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S]. Science 258, 1604-1610.
• Correll, C.C., Ludwig, M.L., Bruns, C.M. and Karplus, P.A. (1993) Structural prototypes for an extended family of flavoprotein reductases: comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxin. Protein Science 2, 2112-2133.
• Deng, Z., Aliverti, A., Zanetti, G., Arakaki, A.K., Ottado, J., Orellano, E.G., Calcaterra, N.B., Ceccarelli, E.A., Carrillo, N. and Karplus, P.A. (1999) A productive NADP⁺ binding mode of ferredoxin-NADP⁺ reductase revealed by protein engineering and crystallographic studies. Nature Struct. Biol. 6, 847-853.
• De Pascalis, A.R., Jelesarov, I., Ackermann, F., Koppenol, W.H., Hirasawa, M., Knaff, D.B. and Bosshard, H.R. (1993) Binding of ferredoxin to ferredoxin:NADP⁺ oxidoreductase: the role of carboxyl groups, electrostatic surface potential, and molecular dipole moment. Protein Science 2, 1126-1135.
• Djordjevic, S., Roberts, D.L., Wang, M., Shea, T., Camitta, M.G.W., Masters, B.S.S. and Kim, J.-J.P. (1995) Crystallization and preliminary x-ray studies of NADPH-cytochrome P450 reductase. Proc. Natl. Acad. Sci. USA 92, 3214-3218.
• Ermler, U., Siddiqui, R.A., Cramm, R. and Friedrich, B. (1995) Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 Å resolution. EMBO J. 14, 6067-6077.
• Gassner, G., Wang, L., Batie, C. and Ballou, D.P. (1994) Reaction of phthalate dioxygenase reductase with NADH and NAD: kinetic and spectral characterization of intermediates. Biochemistry 33, 12184-12193.
• Gruez, A., Zeghouf, M., Bertrand, J., Eschenbrenner, M., Covès, J., Fontecave, M., Pignol, D. and Fontecilla-Camps, J.-C. (1998) The FNR-like domain of the Escherichia coli sulfite reductase flavoprotein component: Crystallization and preliminary X-ray analysis. Acta Crystallogr. D54, 135-136.
• Ingelman, M., Bianchi, V. and Eklund, H. (1997) The three-dimensional structure of flavodoxin reductase from Escherichia coli at 1.7 Å resolution. J. Mol. Biol. 268, 147-157.
• Jelesarov, I., De Pascalis, A.R., Koppenol, W.H., Hirasawa, M., Knaff, D.B. and Bosshard, H.R. (1993) Ferredoxin binding site on ferredoxin:NADP⁺ reductase. Differential chemical modification of free and ferredoxin-bound enzyme. Eur. J. Biochem. 216, 57-66.
• Karplus, P.A. and Bruns, C.M. (1994) Structure-function relations for ferredoxin reductase. J. Bioenerg. Biomembr. 26, 89-99.
• Karplus, P.A., Daniels, M.J. and Herriott, J.R. (1991) Atomic structure of ferredoxin-NADP⁺ reductase: prototype for a structurally novel flavoenzyme family. Science 251, 60-66.
• Kim, J.-J.P., Roberts, D.L., Djordjevic, S., Wang, M., Shea, T.M. and Masters, B.S.S. (1996) Crystallization studies of NADPH-cytochrome P450 reductase. Methods Enzymol. 272, 368-377.
• Lu, G., Campbell, W.H., Schneider, G. and Lindqvist, Y. (1994) Crystal structure of the FAD-containing fragment of corn nitrate reductase at 2.5 Å resolution: relationship to other flavoprotein reductases. Structure 2, 809-821.
• Lu, G., Lindqvist, Y. and Schneider, G. (1995a) A method for processing diffraction data from twinned protein crystals and its application in the structure determination of an FAD/NADH-binding fragment of nitrate reductase. Acta Crystallogr. D51, 13-20.
• Lu, G., Lindqvist, Y., Schneider, G., Dwivedi, U. and Campbell, W.H. (1995b) Structural studies on corn nitrate reductase: refined structure of the cytochrome b reductase fragment at 2.5 Å, its ADP complex and an active-site mutant and modeling of the cytochrome b domain. J. Mol. Biol. 248, 931-948.
• Martínez-Júlvez, M., Medina, M., Hurley, J.K., Hafezi, R., Brodie, T.B., Tollin, G. and Gómez-Moreno, C. (1998a) Lys75 of Anabaena ferredoxin-NADP⁺ reductase is a critical residue for binding ferredoxin and flavodoxin during electron transfer. Biochemistry 37, 13604-13613.
• Martínez-Júlvez, M., Hermoso, J., Hurley, J.K., Mayoral, T., Sanz-Aparicio, J., Tollin, G., Gómez-Moreno, C. and Medina, M. (1998b) Role of Arg100 and Arg264 from Anabaena PCC 7119 ferredoxin-NADP⁺ reductase for optimal NADP⁺ binding and electron transfer. Biochemistry 37, 17680-17691.
• Mayoral, T., Medina, M., Sanz-Aparicio, J., Gómez-Moreno, C. and Hermoso, J.A. (2000) Structural basis of the catalytic role of Glu301 in Anabaena PCC 7119 ferredoxin-NADP+ reductase revealed by x-ray crystallography. Proteins 38, 60-69.
• Medina, M., Martínez-Júlvez, M., Hurley, J.K., Tollin, G. and Gómez-Moreno, C. (1998) Involvement of glutamic acid 301 in the catalytic mechanism of ferredoxin-NADP⁺ reductase from Anabaena PCC 7119. Biochemistry 37, 2715-2728.
• Miki, K., Kaida, S., Kasai, N., Iyanagi, T., Kobayashi, K. and Hayashi, K. (1987) Crystallization and preliminary x-ray crystallographic study of NADH-cytochrome b₅ reductase from pig liver microsomes. J. Biol. Chem. 262, 11801-11802.
• Nishida, H., Inaka, K. and Miki, K. (1995) Specific arrangement of three amino acid residues for flavin-binding barrel structures in NADH-cytochrome b₅ reductase and the other flavin-dependent reductases. FEBS Lett. 361, 97-100.
• Nishida, H., Inaka, K., Yamanaka, M., Kaida, S., Kobayashi, K. and Miki, K. (1995) Crystal structure of NADH-cytochrome b₅ reductase from pig liver at 2.4 Å resolution. Biochemistry 34, 2763-2767.
• Nishida, H. and Miki, K. (1996) Electrostatic properties deduced from refined structures of NADH-cytochrome b₅ reductase and the other flavin-dependent reductases: Pyridine nucleotide-binding and interaction with an electron-transfer partner. Proteins 26, 32-41.
• Prasad, G.S., Kresge, N., Muhlberg, A.B., Shaw, A., Jung, Y.S., Burgess, B.K. and Stout, C.D. (1998) The crystal structure of NADPH:ferredoxin reductase from Azotobacter vinelandii. Protein Science 7, 2541-2549.
• Serre, L., Medina, M., Gómez-Moreno, C., Fontecilla-Camps, J.C. and Frey, M. (1991) Crystals of Anabaena PCC 7119 ferredoxin-NADP⁺ reductase. J. Mol. Biol. 218, 271-272.
• Serre, L., Vellieux, F.M.D., Medina, M., Gómez-Moreno, C., Fontecilla-Camps, J.C. and Frey, M. (1996) X-ray structure of the ferredoxin:NADP⁺ reductase from the cyanobacterium Anabaena PCC 7119 at 1.8 Å resolution, and crystallographic studies of NADP⁺ binding at 2.25 Å resolution. J. Mol. Biol. 263, 20-39.
• Sheriff, S. and Herriott, J.R. (1981) Structure of ferredoxin-NADP oxidoreductase and the location on the NADP binding site. Results at 3.7 Å resolution. J. Mol. Biol. 145, 441-451.
• Zeghouf, M., Fontecave, M., Macherel, D. and Covès, J. (1998) The flavoprotein component of the Escherichia coli sulfite reductase: Expression, purification, and spectral and catalytic properties of a monomeric form containing both the flavin adenine dinucleotide and the flavin mononucleotide cofactors. Biochemistry 37, 6114-6123.

Back to the Directory of P450-containing Systems home page:

Trieste site

Gödöllõ site