Characterisation of flavodoxin NADP+ oxidoreductase and flavodoxin; key components of electron transfer in Escherichia coli

European Journal of Biochemistry

Volumn 257, Issue 3, 1998, Pages 577-585

  McIver, Lisa ^a   Leadbeater, Claire ^a   Campopiano, Dominic J ^a   Baxter, Robert L ^a   Daff, Simon N ^a   Chapman, Stephen K ^a   Munro, Andrew W ^a  

^a UNIVERSITY OF EDINBURGH   (United Kingdom)

Author keywords

Cytochrome P 450; Enzyme kinetics; Flavodoxin; Flavodoxin NADP+ oxidoreductase; Redox potentiometry

Indexed keywords

CYTOCHROME C; CYTOCHROME P450; FLAVODOXIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE DEHYDROGENASE; SEMIQUINONE;

ARTICLE; CROSS LINKING; ELECTRON TRANSPORT; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME STRUCTURE; ESCHERICHIA COLI; ISOELECTRIC POINT; MOLECULAR WEIGHT; NONHUMAN; OXIDATION REDUCTION REACTION; POTENTIOMETRY; PRIORITY JOURNAL;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; FELIS CATUS;

EID: 0032211496     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2570577.x     Document Type: Article

References (32)

1. Sanyal, I., Cohen, G. & Flint, D. H. (1994) Biotin synthase - purification, characterization as a [2Fe-2S] cluster protein, and in vitro activity of the Escherichia coli BioB gene product, Biochemistry 33, 3625-3631.
2. Fujii, K. & Huennekens, F. M. (1974) Activation of methionine synthase by a reduced triphosphopyridine nucleotide-dependent flavoprotein system, J. Biol. Chem. 249, 6745-6750.
3. Blaschkowski, H. P., Neuer, G., Ludwig-Festl, M. & Knappe, J. (1982) Routes of flavodoxin and ferredoxin reduction in Escherichia coli coA acylating pyruvate - flavodoxin and NADPH-flavodoxin oxidoreductases participating in the activation of the pyruvate-formate lyase, Eur. J. Biochem. 123, 563-569.
4. Reichard, P. (1993) The anaerobic ribonucleotide reductase from Escherichia coli, J. Biol. Chem. 268, 8383-8386.
5. Jenkins, C. M. & Waterman, M. R. (1994) Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli support bovine cytochrome P450 c17 hydroxylase activities. J. Biol. Chem. 269, 27401-27408.
6. Mayhew, S. G. & Tollin, G. (1993) General properties of flavodoxins, in Chemistry and biochemistry of flavoenzymes (Müller, F., ed.) pp. 389-426, CRC Press, Boca Raton, Florida.
7. Fujii, K., Galivan, J. H. & Huennekens, F. M. (1977) Activation of methionine synthase: further characterization of the flavoprotein system. Arch. Biochem. Biophys. 178, 662-666.
8. Vetter, H. & Knappe, J. (1971) Flavodoxin and ferredoxin of Escherichia coli, Hoppe-Seylers Physiol. Chem. 352, 433-436.
9. Studier, F. W. & Moffat, B. A. (1986) Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189, 113-130.
10. Yanisch-Perron, C., Viera, J. & Messing, J. (1985) Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33, 103-108.
11. + reductase: activation of Escherichia coli anaerobic ribonucleotide reduction, cloning of the gene (FPR) and overexpression of the protein. J. Bacteriol. 175, 1590-1595.
12. Bianchi, V., Eliasson, R., Fontecave, M., Mulliez, E., Hoover, D. M., Matthews, R. & Reichard, P. (1993) Flavodoxin is required for the activation of the anaerobic ribonucleotide reductase. Biochem. Biophys. Res. Commun. 197, 792-797.
13. Dutton, P. L. (1978) Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron transfer systems. Methods Enzymol. 54, 411-435.
14. Munro, A. W., Malarkey, K., McKnight, J., Thomson, A. J., Kelly, S. M. Price, N. C., Lindsay, J. G., Coggins, J. R. & Miles, J. S. (1994) The role of tryptophan 97 of cytochrome P-450 BM3 from Bacillus megaterium in catalytic function. Biochem. J. 303, 423-428.
15. + reductase. Arch. Biochem. Biophys. 311, 480-486.
16. + oxidoreductase gene of Escherichia coli does not affect anaerobic growth but increases sensitivity to paraquat. J. Bacteriol. 177, 4528-4531.
17. Ingelman, M., Bianchi, V. & Eklund, H. (1997) The 3-dimensional structure of flavodoxin reductase at 1.7 Angstrom resolution, J. Mol. Biol. 268, 147-157.
18. Miles, J. S., Munro, A. W., Rospendowski, B. N., Smith, W. E., McKnight, J. & Thomson, A. J. (1992) Domains of the catalytically self-sufficient cytochrome P-450 BM3: genetic construction, overexpression, purification and spectroscopic characterization, Biochem. J. 288, 503-509.
19. Jenkins, C. M., Genzor, C. G., Fillat, M. F., Waterman, M. R. & Gomez Moreno, C. (1997) Negatively charged Anabaena flavodoxin residues [Asp (144) and Glu (145)] are important for reconstitution of cytochrome P450c17 alpha-hydroxylase, J. Biol. Chem. 272, 22509-22513.
20. Sykes, G. A. & Rogers, L. J. (1984) Redox potentials of algal and cyanobacterial flavodoxins, Biochem. J. 217, 845-850.
21. + and NADPH, J. Biol. Chem. 251, 4299-4306.
22. 6, Biochemistry 16, 2725-2730.
23. Hoover, D. M. & Ludwig, M. L. (1997) A flavodoxin that is required for enzyme activation: the structure of oxidized flavodoxin from E. coli at 1.8 A resolution, Protein Sci. 6, 2525-2537.
24. Wang, M., Roberts, D. L., Paschke, R., Shea, T. M., Masters, B. S. S. & Kim, J.-J. P. (1997) Three dimensional structure of NADPH-cytochrome P-450 reductase: prototype for FMN- and FAD-containing enzymes. Proc. Natl Acad. Sci. USA 94, 8411-8416.
25. Abu-Soud, H. M., Feldman, P. L., Clark, P. & Stuehr, D. J. (1994) Electron transfer in the nitric oxide synthases: characterization of L-arginine analogs that block heme iron reduction, J. Biol. Chem. 269, 32318-32326.
26. Porter, T. D. (1991) An unusual, yet strongly conserved flavoprotein reductase in bacteria and mammals. Trends Biochem. Sci. 16, 154-158.
27. Smith, G. C. M., Tew, D. G. & Wolf, C. R. (1994) Dissection of NADPH-cytochrome P450 oxidoreductase into distinct functional domains, Proc. Natl Acad. Sci. USA 91, 8710-8714.
28. Govindaraj, S. & Poulos, T. L. (1997) The domain architecture of cytochrome P450 BM3, J. Biol. Chem. 272, 7915-7921.
29. Daff, S. N., Chapman, S. K., Turner, K. L., Holt, R. A., Govindaraj, S., Poulos, T. L. & Munro, A. W. (1997) Redox control of the catalytic cycle of cytochrome P-450 BM3, Biochemistry 36, 13816-13823.
30. s reductase, Biochemistry 13, 1701-1710.
31. Massey, V. (1991) A simple method for the determination of redox potentials, in Flavins and flavoproteins 1990 (Curti, B., Ronchi, S. & Zanetti, G., eds) pp. 59-66, Walter de Gruyter, New York.
32. Draper, R. D. & Ingraham, L. L. (1968) A potentiometric study of the flavin semiquinone equilibrium. Arch. Biochem. Biophys. 125, 802-808.