Overexpression, isotopic labeling, and spectral characterization of Enterobacter cloacae nitroreductase

Protein Expression and Purification

Volumn 13, Issue 1, 1998, Pages 53-60

  Koder, Ronald L ^a   Miller, Anne Frances ^a,b  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b JOHNS HOPKINS UNIVERSITY   (United States)

Author keywords

Flavoprotein; Isotopic labeling; Nitroreductase

Indexed keywords

BACTERIAL METABOLISM; CARCINOGENICITY; CIRCULAR DICHROISM SPECTROSCOPY; ENTEROBACTER CLOACAE; FLAVIN MONONUCLEOTIDE COFACTOR; GENE OVEREXPRESSION; ISOTOPE LABELING; MUTAGENICITY; NITROREDUCTASE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

BACTERIA (MICROORGANISMS); ENTEROBACTER CLOACAE;

EID: 0032103853     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1997.0866     Document Type: Article

References (47)

1. Spain J. C. Biodegradation of nitroaromatic compounds. Annu. Rev. Microbiol. 49:1995;523-555.
2. Somerville C. C. Purification and characterization of nitrobenzene nitroreductase fromPseudomonas pseudoalcaligenes. J. Bacteriol. 177:1995;3837-3842.
3. Nishino S. F., Spain J. C. Degradation of nitrobenzene by aPseudomonas pseudoalcaligenes. Appl. Environ. Microbiol. 59:1993;2520-2525.
4. Groenewegen P. E. Novel degradative pathway of 4-nitrobenzoate inComamonas acidovorans. J. Gen. Microbiol. 138:1992;1599-1605.
5. Bridgewater J. A. The bystander effect of the nitroreductase/CB1954 enzyme/prodrug system is due to a cell-permeable metabolite. Hum. Gene Ther. 8:1997;709-717.
6. Bailey S. M. Investigation of alternative prodrugs for use withE. coli. Gene Ther. 3:1996;1143-1150.
7. Bridgewater J. A. Expression of the bacterial nitroreductase enzyme in mammalian cells renders them selectively sensitive to killing by the prodrug CB1954. Eur. J. Cancer. 31A:1995;2362-2670.
8. Knox R. J. Virtual cofactors for anEscherichia coli. Biochem. Pharmacol. 49:1995;1641-1647.
9. Anlezark G. M. Bioactivation of dinitrobenzamide mustards by anE. coli. Biochem. Pharmacol. 50:1995;609-618.
10. Knox R. J. The bioactivation of 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB1954). II. A comparison of anEscherichia coli. Biochem. Pharmacol. 44:1992;2297-2301.
11. Anlezark G. M. The bioactivation of 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB1954). I. Purification and properties of a nitroreductase enzyme fromEscherichia coli. Biochem. Pharmacol. 44:1992;2289-2295.
12. Knox R. J. The bioactivation of CB 1954 and its use as a prodrug in antibody-directed enzyme prodrug therapy (ADEPT). Cancer Metastasis Rev. 12:1993;195-212.
13. Chung K. T. Effects of the nitro-group on the mutagenicity and toxicity of some benzamines. Environ. Mol. Mutagen. 27:1996;67-74.
14. DeMarini D. M. Mutation spectra of chemical fractions of a complex mixture: Role of nitroarenes in the mutagenic specificity of municipal waste incinerator emissions. Mutat. Res. 349:1996;1-20.
15. Sera N. Mutagenicity of nitrophenanthrene derivatives forSalmonella typhimurium. Mutat. Res. 349:1996;137-144.
16. Ball L. M. Metabolic activation of the genotoxic environmental contaminants 2- and 3-nitrofluoranthene in variants ofSalmonella typhimurium. Mutagenesis. 10:1995;497-504.
17. Beland, F. A. 1989, DNA Binding by 1-Nitropyrene and Dinitropyrenesin Vitroin Vivo, Health Effects Institute, 1, 16.
18. Djuric Z. DNA binding by 1-nitropyrene and 1,6-dinitropyrenein vitroin vivo. Carcinogenesis. 9:1988;357-364.
19. Cho B. NMR structural studies of a 15-mer DNA sequence from aras. Biochemistry. 31:1992;9587-9602.
20. Peterson F. J. Oxygen-sensitive and -insensitive nitroreduction byEscherichia coli. J. Biol. Chem. 254:1979;4009-4014.
21. Bryant C., DeLuca M. Purification and characterization of an oxygen-insensitive NAD(P)H nitroreductase fromEnterobacter cloacae. J. Biol. Chem. 266:1991;4119-4125.
22. Bryant C. Cloning, nucleotide sequence, and expression of the nitroreductase gene fromEnterobacter cloacae. J. Biol. Chem. 266:1991;4126-4130.
23. Zenno S., Saigo K. Identification of the genes encoding NAD(P)H-flavin oxidoreductases that are similar in sequence toEscherichia coliPhotorhabdus luminescens, Vibrio fischeri, Vibrio harveyi,Vibrio orientalis. J. Bacteriol. 176:1994;3544-3551.
24. Bryant, C. P. 1990, Purification, Cloning, and Characterization of an Oxygen-Insensitive NAD(P)H Nitroreductase fromEnterobacter Cloacae, UCSD, San Diego, CA.
25. Sanger F. DNA sequencing with chain-terminating inhibitors. Proc. Nat. Acad. Sci. USA. 74:1977;5463-5467.
26. Mainiatis T. Molecular Cloning: A Laboratory Manual. 1982;Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
27. Bensadoun A., Weinstein D. Assay of proteins in the presence of interfering materials. Anal. Biochem. 70:1976;241-250.
28. Orr G. A., Blanchard J. S. High-performance ion-exchange separation of oxidized and reduced nicotinamide adenine dinucleotides. Anal. Biochem. 142:1984;232-234.
29. Russell R. A. The stepwise nitration of toluene. J. Chem. Ed. 67:1990;68-69.
30. Moore J. T. Overcoming inclusion body formation in a high-level expression system. Prot. Exp. Purif. 4:1993;160-163.
31. Neidhardt F. C. Culture medium for enterobacteria. J. Bacteriol. 119:1974;736-747.
32. Dutton P. L. Redox potentiometry: Determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems. Methods Enzymol. 54:1978;411-435.
33. Kay L. E. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114:1992;10663-10665.
34. Delaglio F. NMRPipe: A multidimensional spectral processing system based on UNIX Pipes. J. Biomol. NMR. 6:1995;277-293.
35. Bachmann B. J. Linkage map ofEscherichia coli. Microbiol. Rev. 54:1990;130-197.
36. Koder R. L., Miller A.-F. Biochim. Biophys. Acta. 1997.
37. Visser A., Muller F. Absorption and fluorescence studies on neutral and cationic isoalloxazines. Helv. Chim. Acta. 62:1979;593-608.
38. Koziol J. Studies on flavins in organic solvents. 3. Spectral behaviour of lumiflavin. Photochem. Photobiol. 9:1969;45-53.
39. Lei B. Vibrio harveyi. J. Bacteriol. 176:1994;3552-3558.
40. Zenno S. Gene cloning, purification, and characterization of NfsB, a minor oxygen-insensitive nitroreductase fromEscherichia coli,Vibrio fischeri. J. Biochem. (Tokyo). 120:1996;736-744.
41. Visser A. J. Fluorescence properties of reduced flavins and flavoproteins. Eur. J. Biochem. 101:1979;13-21.
42. Edmondson D. E., Tollin G. Circular dichroism studies of the flavin chromophore and of the relation between redox properties and flavin environment in oxidases and dehydrogenases. Biochemistry. 10:1971;113-124.
43. Ahmed S. A., Claiborne A. The streptococcal flavoprotein NADH oxidase. I. Evidence linking NADH oxidase and NADH peroxidase cysteinyl redox centers. J. Biol. Chem. 264:1989;19856-19863.
44. Maeda-Yorita K. Properties of lipoamide dehydrogenase altered by site-directed mutagenesis at a key residue (I184Y) in the pyridine nucleotide binding domain. Biochemistry. 30:1991;11788-11795.
45. Cantor C., Schimmel P. Biophysical Chemistry. 1980;Freeman, New York.
46. Tollin G. Magnetic circular dichroism and circular dichroism of riboflavin and its analogs. Biochemistry. 7:1968;1720-1727.
47. Muller F. Free flavins: Synthesis, chemical, and physical properties. Chemistry and Biochemistry of Flavoenzymes. 1991;CRC Press, Boca Raton. p. 2-72.