Selected references on NADPH:P450 reductases

Last modified: Thu Apr 15 13:28:55 BST 2004

• Barsukov, I., Modi, S., Lian, L.-Y., Sze, K.H., Paine, M.J.I., Wolf, C.R. and Roberts, G.C.K. (1997) ¹H, ¹⁵N and ¹³C NMR resonance assignment, secondary structure and global fold of the FMN-binding domain of human cytochrome P450 reductase. J. Biomol. NMR 10, 63-75.
• Benveniste, I., Lesot, A., Hasenfratz, M.P., Kochs, G. and Durst, F. (1991) Multiple forms of NADPH-cytochrome P450 reductase in higher plants. Biochem. Biophys. Res. Commun. 177, 105-112.
• Cenas, N., Anusevicius, Z., Bironaite, D., Bachmanova, G.I., Archakov, A.I. and Ollinger, K. (1994) The electron transfer reactions of NADPH:cytochrome P450 reductase with nonphysiological oxidants. Arch. Biochem. Biophys. 315, 400-406.
• Evrard, A., Zeghouf, M., Fontecave, M., Roby, C. and Covès, J. (1999) ³¹P nuclear magnetic resonance study of the flavoprotein component of the Escherichia coli sulfite reductase. Eur. J. Biochem. 261, 430-437.
• Fujii, H. and Kakinuma, K. (1991) Electron transfer reactions in the NADPH oxidase system of neutrophils - involvement of an NADPH-cytochrome c reductase in the oxidase system. Biochim. Biophys. Acta 1095, 201-209.
• Guengerich, F.P. and Johnson, W.W. (1997) Kinetics of ferric cytochrome P450 reduction by NADPH-cytochrome P450 reductase: Rapid reduction in the absence of substrate and variations among cytochrome P450 systems. Biochemistry 36, 14741-14750.
• Gutierrez, A., Lian, L.-Y., Wolf, C.R., Scrutton, N.S. and Roberts, G.C.K. (2001) Stopped-flow kinetic studies of flavin reduction in human cytochrome P450 reductase and its component domains. Biochemistry 40, 1964-1975.
• Hodgson, A.V. and Strobel, H.W. (1996a) Characterization of the FAD binding domain of cytochrome P450 reductase. Arch. Biochem. Biophys. 325, 99-106.
• Hodgson, A.V. and Strobel, H.W. (1996b) Quantitation of FAD-dependent cytochrome P450 reductase activity by photoreduction. Anal. Biochem. 243, 154-157.
• Kurzban, G.P., Howarth, J., Palmer, G. and Strobel, H.W. (1990) NADPH-cytochrome P-450 reductase. Physical properties and redox behavior in the absence of the FAD moiety. J. Biol. Chem. 265, 12272-12279.
• Makovec, T. and Breskvar, K. (1998) Purification and characterization of NADPH-cytochrome P450 reductase from filamentous fungus Rhizopus nigricans. Arch. Biochem. Biophys. 357, 310-316.
• Munro, A.W., Noble, M.A., Robledo, L., Daff, S.N. and Chapman, S.K. (2001) Determination of the redox properties of human NADPH-cytochrome P450 reductase. Biochemistry 40, 1956-1963.
• Murataliev, M.B. and Feyereisen, R. (1999) Mechanism of cytochrome P450 reductase from the house fly: evidence for an FMN semiquinone as electron donor. FEBS Lett. 453, 201-204.
• Murataliev, M.B. and Feyereisen, R. (2000a) Interaction of NADP(H) with oxidized and reduced P450 reductase during catalysis. Studies with nucleotide analogues. Biochemistry 39, 5066-5074.
• Murataliev, M.B. and Feyereisen, R. (2000b) Functional interactions in cytochrome P450_BM3. Evidence that NADP(H) binding controls redox potentials of the flavin cofactors. Biochemistry 39, 12699-12707.
• Murataliev, M.B., Arino, A., Guzov, V.M.and Feyereisen, R. (1999) Kinetic mechanism of cytochrome P450 reductase from the house fly (Musca domestica). Insect Biochem. Mol. Biol. 29, 233-242.
• Narayanasami, R., Otvos, J.D., Kasper, C.B., Shen, A., Rajagopalan, J., McCabe, T.J., Okita, J.R., Hanahan, D.J. and Masters, B.S.S. (1992) ³¹P NMR spectroscopic studies on purified, native and cloned, expressed forms of NADPH-cytochrome P450 reductase. Biochemistry 31, 4210-4218.
• Narayanasami, R., Horowitz, P.M. and Masters, B.S.S. (1995) Flavin-binding and protein structural integrity studies on NADPH-cytochrome P450 reductase are consistent with the presence of distinct domains. Arch. Biochem. Biophys. 316, 267-274.
• O'Leary, K.A., Beck, T.W. and Kasper, C.B. (1994) NADPH cytochrome P-450 oxidoreductase gene: identification and characterization of the promoter region. Arch. Biochem. Biophys. 310, 452-459.
• Otvos, J.D., Krum, D.P. and Masters, B.S.S. (1986) Localization of the free radical on the flavin mononucleotide of the air-stable semiquinone state of NADPH-cytochrome P-450 reductase using ³¹P NMR spectroscopy. Biochemistry 25, 7220-7228.
• Porter, T.D. (1991) An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals. Trends Biochem. Sci. 16, 154-158.
• Porter, T.D. and Kasper, C.B. (1986) NADPH-cytochrome P-450 oxidoreductase: flavin mononucleotide and flavin adenine dinucleotide domains evolved from different flavoproteins. Biochemistry 25, 1682-1687.
• Porter, T.D., Beck, T.W. and Kasper, C.B. (1990) NADPH-cytochrome P-450 oxidoreductase gene organization correlates with structural domains of the protein. Biochemistry 29, 9814-9818.
• Sem, D.S. and Kasper, C.B. (1994) Kinetic mechanism for the model reaction of NADPH-cytochrome P450 oxidoreductase with cytochrome c. Biochemistry 33, 12012-12021.
• Sevrioukova, I.F. and Peterson, J.A. (1995) NADPH-P-450 reductase: Structural and functional comparisons of the eukaryotic and prokaryotic isoforms. Biochimie 77, 562-572.
• Shen, A.L. and Kasper, C.B. (1996) Role of Ser457 of NADPH-cytochrome P450 oxidoreductase in catalysis and control of FAD oxidation-reduction potential. Biochemistry 35, 9451-9459.
• Shen, S. and Strobel, H.W. (1994) Probing the putative cytochrome P450- and cytochrome c-binding sites on NADPH-cytochrome P450 reductase by anti-peptide antibodies. Biochemistry 33, 8807-8812.
• Shet, M.S., Sathasivan, K., Arlotto, M.A., Mehdy, M.C. and Estabrook, R.W. (1993) Purification, characterization, and cDNA cloning of an NADPH-cytochrome P450 reductase from mung bean. Proc. Natl. Acad. Sci. USA 90, 2890-2894.
• Singh, S.P. and Piette, L.H. (1992) Spin-labeling studies of rat liver NADPH-cytochrome P450 reductase: conformation and function relationship. Arch. Biochem. Biophys. 296, 73-80.
• Slepneva, I.A., Sergeeva, S.V. and Khramtsov, V.V. (1995) Reversible inhibition of NADPH-cytochrome P450 reductase by -lipoic acid. Biochem. Biophys. Res. Commun. 214, 1246-1253.
• Smith, G.C., Tew, D.G. and Wolf, C.R. (1994) Dissection of NADPH-cytochrome P450 oxidoreductase into distinct functional domains. Proc. Natl. Acad. Sci. USA 91, 8710-8714.
• Sugiyama, T., Nisimoto, Y., Mason, H.S. and Loehr, T.M. (1985) Flavins of NADPH-cytochrome P-450 reductase: evidence for structural alteration of flavins in their one-electron-reduced semiquinone states from resonance Raman spectroscopy. Biochemistry 24, 3012-3019.
• Wang, M., Roberts, D.L., Paschke, R., Shea, T.M., Masters, B.S.S. and Kim, J.-J.P. (1997) Three-dimensional structure of NADPH-cytochrome P450 reductase: Prototype for FMN- and FAD-containing enzymes. Proc. Natl. Acad. Sci. USA 94, 8411-8416.

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